PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15767436-1 2005 By selecting the R5 human immunodeficiency virus type 1 (HIV-1) strain JR-CSF for efficient use of a CCR5 coreceptor with a badly damaged amino terminus [i.e., CCR5(Y14N)], we previously isolated variants that weakly utilize CCR5(Delta18), a low-affinity mutant lacking the normal tyrosine sulfate-containing amino-terminal region of the coreceptor. tyrosine O-sulfate 281-297 C-C motif chemokine receptor 5 Homo sapiens 101-105 17920626-2 2007 We previously isolated adapted HIV-1(JRCSF) variants that more efficiently use mutant CCR5s, including CCR5(Delta18) lacking the important tyrosine sulfate-containing amino terminus. tyrosine O-sulfate 139-155 C-C motif chemokine receptor 5 Homo sapiens 86-90 17901336-5 2007 Nonetheless, a critical sulfotyrosine on CCR5 and on 412d induces similar structural rearrangements in gp120. tyrosine O-sulfate 24-37 C-C motif chemokine receptor 5 Homo sapiens 41-45 17901336-6 2007 These results now provide a framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry and define a conserved site on gp120, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system. tyrosine O-sulfate 178-191 C-C motif chemokine receptor 5 Homo sapiens 84-88 18952441-0 2008 Tyrosine-sulfate isosteres of CCR5 N-terminus as tools for studying HIV-1 entry. tyrosine O-sulfate 0-16 C-C motif chemokine receptor 5 Homo sapiens 30-34 18952441-1 2008 The HIV-1 co-receptor CCR5 possesses sulfo-tyrosine (TYS) residues at its N-terminus (Nt) that are required for binding HIV-1 gp120 and mediating viral entry. tyrosine O-sulfate 37-51 C-C motif chemokine receptor 5 Homo sapiens 22-26 18952441-1 2008 The HIV-1 co-receptor CCR5 possesses sulfo-tyrosine (TYS) residues at its N-terminus (Nt) that are required for binding HIV-1 gp120 and mediating viral entry. tyrosine O-sulfate 53-56 C-C motif chemokine receptor 5 Homo sapiens 22-26 18952441-2 2008 By using a 14-residue fragment of CCR5 Nt containing two TYS residues, we recently showed that CCR5 Nt binds gp120 through a conserved region specific for TYS moieties and suggested that this site may represent a target for inhibitors and probes of HIV-1 entry. tyrosine O-sulfate 57-60 C-C motif chemokine receptor 5 Homo sapiens 34-38 18952441-2 2008 By using a 14-residue fragment of CCR5 Nt containing two TYS residues, we recently showed that CCR5 Nt binds gp120 through a conserved region specific for TYS moieties and suggested that this site may represent a target for inhibitors and probes of HIV-1 entry. tyrosine O-sulfate 57-60 C-C motif chemokine receptor 5 Homo sapiens 95-99 18952441-2 2008 By using a 14-residue fragment of CCR5 Nt containing two TYS residues, we recently showed that CCR5 Nt binds gp120 through a conserved region specific for TYS moieties and suggested that this site may represent a target for inhibitors and probes of HIV-1 entry. tyrosine O-sulfate 155-158 C-C motif chemokine receptor 5 Homo sapiens 34-38 18952441-2 2008 By using a 14-residue fragment of CCR5 Nt containing two TYS residues, we recently showed that CCR5 Nt binds gp120 through a conserved region specific for TYS moieties and suggested that this site may represent a target for inhibitors and probes of HIV-1 entry. tyrosine O-sulfate 155-158 C-C motif chemokine receptor 5 Homo sapiens 95-99 18952441-3 2008 As peptides containing sulfo-tyrosines are difficult to synthesize and handle due to limited stability of the sulfo-ester moiety, we have now incorporated TYS isosteres into CCR5 Nt analogs and assessed their binding to a complex of gp120-CD4 using saturation transfer difference (STD) NMR and surface plasmon resonance (SPR). tyrosine O-sulfate 155-158 C-C motif chemokine receptor 5 Homo sapiens 174-178 18952441-5 2008 STD enhancements for phosphotyrosine-containing CCR5 Nt analogs were greatly diminished consistent with earlier findings showing sulfo-tyrosine to be essential for CCR5 Nt binding to gp120. tyrosine O-sulfate 129-143 C-C motif chemokine receptor 5 Homo sapiens 48-52 18952441-5 2008 STD enhancements for phosphotyrosine-containing CCR5 Nt analogs were greatly diminished consistent with earlier findings showing sulfo-tyrosine to be essential for CCR5 Nt binding to gp120. tyrosine O-sulfate 129-143 C-C motif chemokine receptor 5 Homo sapiens 164-168 15767436-1 2005 By selecting the R5 human immunodeficiency virus type 1 (HIV-1) strain JR-CSF for efficient use of a CCR5 coreceptor with a badly damaged amino terminus [i.e., CCR5(Y14N)], we previously isolated variants that weakly utilize CCR5(Delta18), a low-affinity mutant lacking the normal tyrosine sulfate-containing amino-terminal region of the coreceptor. tyrosine O-sulfate 281-297 C-C motif chemokine receptor 5 Homo sapiens 160-164 15767436-1 2005 By selecting the R5 human immunodeficiency virus type 1 (HIV-1) strain JR-CSF for efficient use of a CCR5 coreceptor with a badly damaged amino terminus [i.e., CCR5(Y14N)], we previously isolated variants that weakly utilize CCR5(Delta18), a low-affinity mutant lacking the normal tyrosine sulfate-containing amino-terminal region of the coreceptor. tyrosine O-sulfate 281-297 C-C motif chemokine receptor 5 Homo sapiens 160-164 12169668-5 2002 We found that CCR5 2-18 is sulfated by both TPST isoenzymes leading to a final product with four sulfotyrosine residues. tyrosine O-sulfate 97-110 C-C motif chemokine receptor 5 Homo sapiens 14-18 32693837-5 2020 Structural alignment with gp120 in complex with the co-receptor CCR5 indicates that the new pocket corresponds to TYS at position 15 of CCR5. tyrosine O-sulfate 114-117 C-C motif chemokine receptor 5 Homo sapiens 64-68 11733580-6 2001 Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5. tyrosine O-sulfate 102-119 C-C motif chemokine receptor 5 Homo sapiens 185-189 11356961-2 2001 Sulfotyrosine and other negatively charged residues in the CCR5 amino-terminal domain (Nt) are crucial for gp120 binding and viral entry. tyrosine O-sulfate 0-13 C-C motif chemokine receptor 5 Homo sapiens 59-63 11356961-3 2001 We previously showed that a soluble gp120-CD4 complex specifically binds to a peptide corresponding to CCR5 Nt residues 2 to 18, with sulfotyrosines in positions 10 and 14. tyrosine O-sulfate 134-148 C-C motif chemokine receptor 5 Homo sapiens 103-107 10823934-0 2000 Specific interaction of CCR5 amino-terminal domain peptides containing sulfotyrosines with HIV-1 envelope glycoprotein gp120. tyrosine O-sulfate 71-85 C-C motif chemokine receptor 5 Homo sapiens 24-28 10823934-2 2000 Acidic residues and sulfotyrosines in the amino-terminal domain (Nt) of CCR5 are crucial for viral fusion and entry. tyrosine O-sulfate 20-34 C-C motif chemokine receptor 5 Homo sapiens 72-76 10823934-6 2000 The gp120/CD4 complexes containing envelope glycoproteins from isolates that use CCR5 as a coreceptor associated with Nt peptides containing sulfotyrosines but not with peptides containing sulfotyrosines in scrambled Nt sequences. tyrosine O-sulfate 141-155 C-C motif chemokine receptor 5 Homo sapiens 81-85 32693837-5 2020 Structural alignment with gp120 in complex with the co-receptor CCR5 indicates that the new pocket corresponds to TYS at position 15 of CCR5. tyrosine O-sulfate 114-117 C-C motif chemokine receptor 5 Homo sapiens 136-140 22547820-6 2012 Quantitative microscopy of 2G12 binding and dissociation from single virions and studies using a split CCR5 coreceptor suggest that 2G12 competitively inhibits interactions between gp120"s V3 loop and the tyrosine sulfate-containing CCR5 amino terminus, thereby reducing assembly of complexes that catalyze entry. tyrosine O-sulfate 205-221 C-C motif chemokine receptor 5 Homo sapiens 233-237 21793507-2 2011 After engaging the CD4 receptor at the cell surface, the HIV-1 gp120 glycoprotein binds to the CCR5 co-receptor via an interaction that requires two tyrosine sulfates, at positions 10 and 14 in the CCR5-N terminus. tyrosine O-sulfate 149-166 C-C motif chemokine receptor 5 Homo sapiens 95-99 21793507-2 2011 After engaging the CD4 receptor at the cell surface, the HIV-1 gp120 glycoprotein binds to the CCR5 co-receptor via an interaction that requires two tyrosine sulfates, at positions 10 and 14 in the CCR5-N terminus. tyrosine O-sulfate 149-166 C-C motif chemokine receptor 5 Homo sapiens 198-202 21793507-4 2011 A class of tyrosine sulfate-mimicking small molecules containing a "phenyl sulfonate-linker-aromatic" motif was identified that specifically inhibited binding of gp120 to the CCR5-N terminus as well as to sulfated antibodies that recognize the co-receptor binding region on gp120. tyrosine O-sulfate 11-27 C-C motif chemokine receptor 5 Homo sapiens 175-179