PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20739067-0 2010 CD4 dimerization requires two cysteines in the cytoplasmic domain of the molecule and occurs in microdomains distinct from lipid rafts. Cysteine 30-39 CD4 molecule Homo sapiens 0-3 25253346-18 2014 We used the atomic-level structure to reengineer gp120 cores to preferentially present the cysteine-stabilized CD4bs and to mask (by glycan) nonneutralizing determinants. Cysteine 91-99 CD4 molecule Homo sapiens 111-114 22355778-0 2012 Activated human CD4+ T cells express transporters for both cysteine and cystine. Cysteine 59-67 CD4 molecule Homo sapiens 16-19 20974843-2 2010 CD4 exists in three different forms on the cell surface defined by the state of the domain 2 cysteine residues: an oxidized monomer, a reduced monomer, and a covalent dimer linked through the domain 2 cysteines. Cysteine 93-101 CD4 molecule Homo sapiens 0-3 20974843-2 2010 CD4 exists in three different forms on the cell surface defined by the state of the domain 2 cysteine residues: an oxidized monomer, a reduced monomer, and a covalent dimer linked through the domain 2 cysteines. Cysteine 201-210 CD4 molecule Homo sapiens 0-3 20739067-4 2010 Our results indicated that within the cytoplasmic tail of CD4, two cysteines played a crucial role in the dimers formation, since point mutations or truncation upstream of these residues prevented dimerization. Cysteine 67-76 CD4 molecule Homo sapiens 58-61 20739067-8 2010 Together, these findings demonstrate that two cysteines within the CD4 cytoplasmic tail are critical for dimerization, that CD4 dimers locate preferentially in microdomains distinct than classical lipid rafts, likely tetraspanin-enriched microdomains, and that CD4 dimers are implicated in the process of HIV infection. Cysteine 46-55 CD4 molecule Homo sapiens 67-70 19781520-7 2010 In the present work, we describe the NOE-based solution structure of the transmembrane and cytoplasmic domains of the cystein-free variant of CD4 (CD4mut) in dodecylphosphocholine (DPC) micelles. Cysteine 118-125 CD4 molecule Homo sapiens 142-145 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 44-47 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 44-47 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 127-130 CD4 molecule Homo sapiens 44-47 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 127-130 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 127-130 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 44-47 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 97-100 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Cysteine 197-200 CD4 molecule Homo sapiens 44-47 19781520-7 2010 In the present work, we describe the NOE-based solution structure of the transmembrane and cytoplasmic domains of the cystein-free variant of CD4 (CD4mut) in dodecylphosphocholine (DPC) micelles. Cysteine 118-125 CD4 molecule Homo sapiens 147-153 16622019-1 2006 We have studied the human CD4 T cell response to a functionally conserved domain of Plasmodium falciparum erythrocyte membrane protein-1, cysteine interdomain region-1alpha (CIDR-1alpha). Cysteine 138-146 CD4 molecule Homo sapiens 26-29 18035040-4 2007 The five cysteine residues of this region have been replaced with serine and histidine residues in the polypeptide CD4mut. Cysteine 9-17 CD4 molecule Homo sapiens 115-121 18193050-4 2008 Inhibition of CD4+ T cell activation by HVEM-transfected cells was dependent on CD160 and BTLA; when the cysteine-rich domain 1 of HVEM was deleted, this inhibition was lost, resulting in strong T cell activation. Cysteine 105-113 CD4 molecule Homo sapiens 14-17 17067272-7 2006 Initial functional analysis demonstrated that envelope proteins with 19 cysteine residues bind to CD4 and the CCR5 chemokine coreceptor, and are infectious. Cysteine 72-80 CD4 molecule Homo sapiens 98-101 16480776-6 2006 In addition, bat CD4 lacked cystein, which suggested that the disulfide bond could not be formed. Cysteine 28-35 CD4 molecule Homo sapiens 17-20 12517957-1 2003 By mutagenesis, we demonstrated that the palmitoylation of the membrane-proximal Cys(396) and Cys(399)of CD4, and the association of CD4 with Lck contribute to the enrichment of CD4 in lipid rafts. Cysteine 81-84 CD4 molecule Homo sapiens 105-108 15322779-4 2004 Unlike avian and mammalian CD4, fugu CD4 lacks the Cys pair of the first Ig-like domain, but has a unique possible disulfide bond in the third domain. Cysteine 51-54 CD4 molecule Homo sapiens 37-40 14764741-11 2004 Overall, these results indicate that vaccination with class I tumor peptides can induce HLA-DR-restricted CD4(+) T cells in vivo and elicit humoral immune responses, and that a cysteine-containing peptide can be recognized by CD4(+) T cells not only as a monomer, but also as a dimer. Cysteine 177-185 CD4 molecule Homo sapiens 106-109 14764741-11 2004 Overall, these results indicate that vaccination with class I tumor peptides can induce HLA-DR-restricted CD4(+) T cells in vivo and elicit humoral immune responses, and that a cysteine-containing peptide can be recognized by CD4(+) T cells not only as a monomer, but also as a dimer. Cysteine 177-185 CD4 molecule Homo sapiens 226-229 12517957-1 2003 By mutagenesis, we demonstrated that the palmitoylation of the membrane-proximal Cys(396) and Cys(399)of CD4, and the association of CD4 with Lck contribute to the enrichment of CD4 in lipid rafts. Cysteine 94-97 CD4 molecule Homo sapiens 105-108 9830036-2 1998 Association of p56(lck) with CD4 requires two conserved cysteine residues in the cytosolic domain of CD4 and two in the amino terminus of p56(lck), consistent with the notion that these four residues coordinate a single metal atom (1-5). Cysteine 56-64 CD4 molecule Homo sapiens 29-32 10831377-6 2000 CD4(+) expression was significantly decreased when metacestode E/S products and L-cysteine were added to lymphocyte cultures (P = 0.027). Cysteine 80-90 CD4 molecule Homo sapiens 0-3 12231211-1 2002 We designed a new class of aromatically modified exocyclic peptides based on the structure of CD4 by engineering one of the cysteine residues in a peptidomimetic derived from the CDR3 region of the CD4 molecule. Cysteine 124-132 CD4 molecule Homo sapiens 94-97 12231211-1 2002 We designed a new class of aromatically modified exocyclic peptides based on the structure of CD4 by engineering one of the cysteine residues in a peptidomimetic derived from the CDR3 region of the CD4 molecule. Cysteine 124-132 CD4 molecule Homo sapiens 198-201 11737067-0 2001 Recognition of the 60 kilodalton cysteine-rich outer membrane protein OMP2 by CD4(+) T cells from humans infected with Chlamydia trachomatis. Cysteine 33-41 CD4 molecule Homo sapiens 78-81 9830036-2 1998 Association of p56(lck) with CD4 requires two conserved cysteine residues in the cytosolic domain of CD4 and two in the amino terminus of p56(lck), consistent with the notion that these four residues coordinate a single metal atom (1-5). Cysteine 56-64 CD4 molecule Homo sapiens 101-104 9391913-2 1997 As the NQGSF sequence, corresponding to the 39-43 fragment of human CD4 protein, was found to be involved in the HIV gp120 interaction, it has been synthesized in a cyclic form by adding two cysteine residues at the amino and carboxy termini. Cysteine 191-199 CD4 molecule Homo sapiens 68-71 9868910-7 1998 In addition, the two sets of isolated consecutive amino acid residues in Cys(Bzl)84-CD4 (81-92) and hirudin (54-56) yielded internal ions from the cleavages at the (O=C)-NH bond between the acidic residues. Cysteine 73-76 CD4 molecule Homo sapiens 84-87 9603449-6 1998 Moreover, inhibitory signals were transduced in HSB-2 CD4mut cells expressing a cell surface CD4 with a double cysteine mutation in its cytoplasmic tail that renders the molecule unable to bind p56lck, but not HSB-2 CD4.402 cells expressing a truncated form of CD4 which lacks the cytoplasmic domain. Cysteine 111-119 CD4 molecule Homo sapiens 54-57 9603449-6 1998 Moreover, inhibitory signals were transduced in HSB-2 CD4mut cells expressing a cell surface CD4 with a double cysteine mutation in its cytoplasmic tail that renders the molecule unable to bind p56lck, but not HSB-2 CD4.402 cells expressing a truncated form of CD4 which lacks the cytoplasmic domain. Cysteine 111-119 CD4 molecule Homo sapiens 93-96 9603449-6 1998 Moreover, inhibitory signals were transduced in HSB-2 CD4mut cells expressing a cell surface CD4 with a double cysteine mutation in its cytoplasmic tail that renders the molecule unable to bind p56lck, but not HSB-2 CD4.402 cells expressing a truncated form of CD4 which lacks the cytoplasmic domain. Cysteine 111-119 CD4 molecule Homo sapiens 93-96 9603449-6 1998 Moreover, inhibitory signals were transduced in HSB-2 CD4mut cells expressing a cell surface CD4 with a double cysteine mutation in its cytoplasmic tail that renders the molecule unable to bind p56lck, but not HSB-2 CD4.402 cells expressing a truncated form of CD4 which lacks the cytoplasmic domain. Cysteine 111-119 CD4 molecule Homo sapiens 93-96 9582308-10 1998 Finally, this domain contains a Cys-X-X-Cys sequence that resembles that of p56(lck), which is responsible for the interaction with the cytoplasmic tails of CD4 and CD8. Cysteine 32-35 CD4 molecule Homo sapiens 157-160 9582308-10 1998 Finally, this domain contains a Cys-X-X-Cys sequence that resembles that of p56(lck), which is responsible for the interaction with the cytoplasmic tails of CD4 and CD8. Cysteine 40-43 CD4 molecule Homo sapiens 157-160 7806282-1 1995 The T-lymphocyte co-receptors of MHC glycoproteins CD4 and CD8 are known to be associated with the protein tyrosine kinase Lck via cysteine-containing sequences in the cytoplasmic domains of CD4 and CD8 and in the N-terminal domain of Lck. Cysteine 131-139 CD4 molecule Homo sapiens 51-54 8707860-11 1996 Thus, the intracellular location of cysteine transport activity may be cell lineage-dependent, and its presence may, in part, determine whether an organelle is a productive site of processing antigens with disulfide bonds that is necessary for CD4+ cell activation. Cysteine 36-44 CD4 molecule Homo sapiens 244-247 8551242-3 1996 Apoptosis, but not HIV replication, was abrogated by deleting the NH2-terminal intracytoplasmic tail of CD4, or by mutating the two critical cysteines in this tail that are responsible for CD4-p56lck interaction. Cysteine 141-150 CD4 molecule Homo sapiens 189-192 7806282-1 1995 The T-lymphocyte co-receptors of MHC glycoproteins CD4 and CD8 are known to be associated with the protein tyrosine kinase Lck via cysteine-containing sequences in the cytoplasmic domains of CD4 and CD8 and in the N-terminal domain of Lck. Cysteine 131-139 CD4 molecule Homo sapiens 191-194 8151774-5 1994 Our results indicate that the portion of the cytoplasmic domain required for the down-regulation of CD4 by Nef overlaps with the binding site of p56lck, but the cysteine residues which are essential for the association of CD4 with p56lck are not required. Cysteine 161-169 CD4 molecule Homo sapiens 100-103 8188754-3 1994 However, the sequence conservation of this cytoplasmic domain and its abundance of cysteine residues, reminiscent of the cytoplasmic domains of CD4 and CD8, suggest a biological function. Cysteine 83-91 CD4 molecule Homo sapiens 144-147 8151774-5 1994 Our results indicate that the portion of the cytoplasmic domain required for the down-regulation of CD4 by Nef overlaps with the binding site of p56lck, but the cysteine residues which are essential for the association of CD4 with p56lck are not required. Cysteine 161-169 CD4 molecule Homo sapiens 222-225 1985197-7 1991 Mutation of the putative disulfide bridge-forming Cys at residue 336 blocked gp160 cleavage and CD4 binding. Cysteine 50-53 CD4 molecule Homo sapiens 96-99 1671341-1 1991 The T cell-specific transmembrane glycoprotein CD4 interacts with class II MHC molecules via its external domain and is associated with tyrosine kinase p56lck via a cysteine motif in its cytoplasmic domain. Cysteine 165-173 CD4 molecule Homo sapiens 47-50 8112293-8 1994 Results from experiments with a CD4 construct containing mutations of the cysteine residues which are responsible for association of CD4 with p56lck demonstrate that p56lck is implicated in the transduction of the signal negatively regulating HIV replication. Cysteine 74-82 CD4 molecule Homo sapiens 32-35 8112293-8 1994 Results from experiments with a CD4 construct containing mutations of the cysteine residues which are responsible for association of CD4 with p56lck demonstrate that p56lck is implicated in the transduction of the signal negatively regulating HIV replication. Cysteine 74-82 CD4 molecule Homo sapiens 133-136 8335927-7 1993 Analysis of mutant p56lck recombinant proteins showed that two cysteine residues critical for p56lck-CD4 (or -CD8) complex formation are also required for the p56lck-4-1BB interaction. Cysteine 63-71 CD4 molecule Homo sapiens 101-104 1618861-5 1992 Mutations of each of 2 cysteine residues, Cys394 and Cys397, in CD4 at the junction of the transmembrane and cytoplasmic domains reduced labeling with [3H]palmitic acid, and mutation of both cysteines eliminated labeling. Cysteine 23-31 CD4 molecule Homo sapiens 64-67 1618861-5 1992 Mutations of each of 2 cysteine residues, Cys394 and Cys397, in CD4 at the junction of the transmembrane and cytoplasmic domains reduced labeling with [3H]palmitic acid, and mutation of both cysteines eliminated labeling. Cysteine 191-200 CD4 molecule Homo sapiens 64-67 2045792-5 1991 CD4-binding and syncytium formation assays demonstrated that the disulphide bridge of cysteine 402 stabilized a conformation essential for receptor binding as well as syncytium formation by CD4+ cells. Cysteine 86-94 CD4 molecule Homo sapiens 0-3 2045792-5 1991 CD4-binding and syncytium formation assays demonstrated that the disulphide bridge of cysteine 402 stabilized a conformation essential for receptor binding as well as syncytium formation by CD4+ cells. Cysteine 86-94 CD4 molecule Homo sapiens 190-193 2000396-2 1991 Seven other truncation mutants of CD4 were expressed well on the cell surface, thus suggesting that the C-terminal amino acids of CD4.Q421stop (-Ser-Glu-Lys-Lys-Thr-Cys) may have the sequence information for ER retention. Cysteine 165-168 CD4 molecule Homo sapiens 34-37 2000396-2 1991 Seven other truncation mutants of CD4 were expressed well on the cell surface, thus suggesting that the C-terminal amino acids of CD4.Q421stop (-Ser-Glu-Lys-Lys-Thr-Cys) may have the sequence information for ER retention. Cysteine 165-168 CD4 molecule Homo sapiens 130-142 2109184-3 1990 The common sequence motif shared by CD4 and CD8 alpha contains two cysteines, and mutation of either cysteine in the CD4 sequence eliminated binding of p56lck.p56lck also contains two cysteine residues within its CD4-CD8 alpha-binding domain, and both are critical to the interaction with CD4 or CD8 alpha. Cysteine 67-76 CD4 molecule Homo sapiens 36-39 2109184-3 1990 The common sequence motif shared by CD4 and CD8 alpha contains two cysteines, and mutation of either cysteine in the CD4 sequence eliminated binding of p56lck.p56lck also contains two cysteine residues within its CD4-CD8 alpha-binding domain, and both are critical to the interaction with CD4 or CD8 alpha. Cysteine 67-75 CD4 molecule Homo sapiens 36-39 2109184-3 1990 The common sequence motif shared by CD4 and CD8 alpha contains two cysteines, and mutation of either cysteine in the CD4 sequence eliminated binding of p56lck.p56lck also contains two cysteine residues within its CD4-CD8 alpha-binding domain, and both are critical to the interaction with CD4 or CD8 alpha. Cysteine 101-109 CD4 molecule Homo sapiens 117-120 2109184-3 1990 The common sequence motif shared by CD4 and CD8 alpha contains two cysteines, and mutation of either cysteine in the CD4 sequence eliminated binding of p56lck.p56lck also contains two cysteine residues within its CD4-CD8 alpha-binding domain, and both are critical to the interaction with CD4 or CD8 alpha. Cysteine 101-109 CD4 molecule Homo sapiens 117-120 2109184-3 1990 The common sequence motif shared by CD4 and CD8 alpha contains two cysteines, and mutation of either cysteine in the CD4 sequence eliminated binding of p56lck.p56lck also contains two cysteine residues within its CD4-CD8 alpha-binding domain, and both are critical to the interaction with CD4 or CD8 alpha. Cysteine 101-109 CD4 molecule Homo sapiens 117-120 2850890-6 1988 The binding of gp120 to CD4 is dependent upon intact sulfhydryl bonds within cysteine residues and glycosylation. Cysteine 77-85 CD4 molecule Homo sapiens 24-27 2558637-0 1989 Cystein 402 of HIV gp 120 is essential for CD4-binding and resistance of gp 120 to intracellular degradation. Cysteine 0-7 CD4 molecule Homo sapiens 43-46 2959511-3 1987 The formation of these oligonuclear complexes designated as Cd4- and Cd3-cluster has now been monitored in MT reconstituted with varying amounts of Cd using differential modification of Cys with 14C-iodoacetamide. Cysteine 186-189 CD4 molecule Homo sapiens 60-63 2959511-8 1987 The extent of labelling of the different Cys in Cd7-MT indicates that the ligands of the Cd3-cluster are three times as accessible to iodoacetamide as those of the Cd4-cluster, suggesting a greater thermodynamic stability of the latter. Cysteine 41-44 CD4 molecule Homo sapiens 164-167 30724942-5 2019 At pH 5, cysteine bridged Cd4(SCYS)11 clusters form. Cysteine 9-17 CD4 molecule Homo sapiens 26-29 3707924-7 1986 The formation of these oligonuclear complexes designated as Cd4 and Cd3 clusters has now been monitored in MT reconstituted with varying amounts of Cd by using differential chemical modification of Cys with [14C]iodoacetamide. Cysteine 198-201 CD4 molecule Homo sapiens 60-63 3707924-12 1986 The extent of labeling of the different Cys in Cd7-MT indicates that the ligands of the Cd3 cluster are 3 times as accessible to iodoacetamide than those of the Cd4 cluster, suggesting a greater thermodynamic or kinetic stability of the latter. Cysteine 40-43 CD4 molecule Homo sapiens 161-164