PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9385632-3 1997 In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. Proline 147-150 peptidylprolyl isomerase A Homo sapiens 165-178 9385632-2 1997 We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex. Proline 54-57 peptidylprolyl isomerase A Homo sapiens 105-118 9385632-2 1997 We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex. Proline 54-57 peptidylprolyl isomerase A Homo sapiens 178-182 9385632-3 1997 In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. Proline 23-30 peptidylprolyl isomerase A Homo sapiens 165-178 9385632-3 1997 In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. Proline 147-150 peptidylprolyl isomerase A Homo sapiens 82-86 9385632-5 1997 Comparison with the recently determined structures of CypA in complexes with larger fragments of the HIV-1 capsid protein demonstrates that CypA recognition of these hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences. Proline 244-247 peptidylprolyl isomerase A Homo sapiens 140-144 9223641-7 1997 These studies reveal that the active site of CypA, which can catalyze the isomerization of proline residues in vitro, also functions as a sequence-specific, protein-binding motif in HIV-1 replication. Proline 91-98 peptidylprolyl isomerase A Homo sapiens 45-49 9261445-3 1997 The incorporation of CyPA into HIV-1 virions is mediated by a specific interaction with a proline-containing, solvent-exposed loop in the capsid (CA) domain of the Gag polyprotein. Proline 90-97 peptidylprolyl isomerase A Homo sapiens 21-25 34099711-4 2021 We demonstrate that proline/arginine repeat polymers inhibit the folding catalyst activity of PPIA, an abundant molecular chaperone and prolyl isomerase in the brain that is altered in amyotrophic lateral sclerosis. Proline 20-27 peptidylprolyl isomerase A Homo sapiens 94-98 9032343-2 1997 Elucidation of the biochemical role of CyPA would be aided by a detailed analysis of the genetic requirements for the formation of the Gag-CyPA complex; previous experiments have demonstrated the requirement for a critical proline and the immediately preceding glycine, located within the capsid domain of Gag, but nothing is known about the necessary CyPA residues. Proline 223-230 peptidylprolyl isomerase A Homo sapiens 39-43 9032343-7 1997 These studies indicate that, as with other proline-containing peptides or cyclosporine A, HIV-1 Gag directly contacts residues in the hydrophobic pocket of CyPA. Proline 43-50 peptidylprolyl isomerase A Homo sapiens 156-160 1453463-9 1992 In addition, CyP A is a closed beta-barrel so that neither the immunosuppressive drug cyclosporin A (CsA) nor the proline-containing substrate can bind to the hydrophobic core of the CyP A barrel, while the hydrophobic core of most other barrels is open for ligation. Proline 114-121 peptidylprolyl isomerase A Homo sapiens 13-18 34099711-5 2021 NMR spectroscopy reveals that proline/arginine repeat polymers bind to the active site of PPIA. Proline 30-37 peptidylprolyl isomerase A Homo sapiens 90-94 22345441-8 2012 The two prolines (P310 and P341 of Japanese fulminant hepatitis 1 [JFH-1]) contained in these motifs, as well as a conserved tryptophan in the spacer region, were required for CyPA binding, HCV replication, and CPI resistance. Proline 8-16 peptidylprolyl isomerase A Homo sapiens 176-180 22973029-3 2012 CyPA binds to proline residues in the C-terminal half of NS5A, in a distributed fashion, and modulates the structure of the disordered domains II and III. Proline 14-21 peptidylprolyl isomerase A Homo sapiens 0-4 31315928-4 2019 NS5A-D2 comprises a short structural motif (PW-turn) embedded in a proline-rich sequence, whose interaction with the human prolyl isomerase cyclophilin A (CypA) is essential for viral RNA replication. Proline 67-74 peptidylprolyl isomerase A Homo sapiens 140-153 31315928-4 2019 NS5A-D2 comprises a short structural motif (PW-turn) embedded in a proline-rich sequence, whose interaction with the human prolyl isomerase cyclophilin A (CypA) is essential for viral RNA replication. Proline 67-74 peptidylprolyl isomerase A Homo sapiens 155-159 24991000-3 2014 Inspection of the CA sequences of lentiviruses reveals that several species of simian immunodeficiency viruses (SIVs) have lost the glycine-proline motif in the helix 4-5 loop important for CypA binding; instead, the helix 4-5 loop in these SIVs exhibits an increase in the number of glutamine residues. Proline 140-147 peptidylprolyl isomerase A Homo sapiens 190-194 23342381-7 2012 Furthermore, a 15 amino acid long peptide fused N terminally to GFP coding sequences confirmed involvement of proline at 310 in CypA binding. Proline 110-117 peptidylprolyl isomerase A Homo sapiens 128-132 23342381-8 2012 Our findings are consistent with CypA acting on multiple prolines outside of the previously identified CypA binding sites. Proline 57-65 peptidylprolyl isomerase A Homo sapiens 33-37 22345441-9 2012 Together, these data provide a high-resolution mapping of proline residues important for CyPA binding and identify critical amino acids modulating HCV susceptibility to the clinical CPI Alisporivir. Proline 58-65 peptidylprolyl isomerase A Homo sapiens 89-93 22342556-4 2012 2D (1)H nuclear magnetic resonance analysis of full-length HIV-1 p6 and p6 peptides established that cyclophilin A (CypA) interacts as a peptidyl-prolyl cis/trans isomerase with all proline residues of p6. Proline 182-189 peptidylprolyl isomerase A Homo sapiens 101-114 22342556-4 2012 2D (1)H nuclear magnetic resonance analysis of full-length HIV-1 p6 and p6 peptides established that cyclophilin A (CypA) interacts as a peptidyl-prolyl cis/trans isomerase with all proline residues of p6. Proline 182-189 peptidylprolyl isomerase A Homo sapiens 116-120 20886100-5 2010 Five independent selections revealed related mutations in a single dipeptide motif (D316 and Y317) located in a proline-rich region of NS5A domain II, which has been implicated in CyPA binding. Proline 112-119 peptidylprolyl isomerase A Homo sapiens 180-184 21963115-3 2011 In this study we investigate whether the notoriously low affinity inhibitory interaction of linear proline-containing peptides with the active site of CypA can be increased through a combination of a high cis/trans ratio and a negatively charged C-terminus as has been recently reported for Trp-Gly-Pro. Proline 99-106 peptidylprolyl isomerase A Homo sapiens 151-155 20920334-5 2010 NMR data at atomic resolution indicate prolyl cis/trans isomerisation of the highly conserved proline residues Pro-5, -10, -14 and -35 of Vpr are catalyzed by human CypA and require only very low concentrations of the isomerase relative to that of the peptide substrates. Proline 94-101 peptidylprolyl isomerase A Homo sapiens 165-169 20920334-5 2010 NMR data at atomic resolution indicate prolyl cis/trans isomerisation of the highly conserved proline residues Pro-5, -10, -14 and -35 of Vpr are catalyzed by human CypA and require only very low concentrations of the isomerase relative to that of the peptide substrates. Proline 111-114 peptidylprolyl isomerase A Homo sapiens 165-169 20920334-8 2010 CONCLUSIONS: Only N-terminal peptides of Vpr containing Pro-35, which appears to be vital for manifold functions of Vpr, bind to CypA in a biosensor assay. Proline 56-59 peptidylprolyl isomerase A Homo sapiens 129-133 20920334-9 2010 This indicates that Pro-35 is essential for a specific CypA-Vpr binding interaction, in contrast to the general prolyl cis/trans isomerisation observed for all proline residues of Vpr, which only involve transient enzyme-substrate interactions. Proline 20-23 peptidylprolyl isomerase A Homo sapiens 55-59 22185200-10 2011 A non-proline-containing 16-residue region of C-terminal Vpr which binds specifically to CypA with similar high affinity as full-length Vpr has been identified. Proline 6-13 peptidylprolyl isomerase A Homo sapiens 89-93 22185200-11 2011 The fact that this is the first non-proline containing binding motif of any protein found to bind to CypA, changes the view on how CypA is able to interact with other proteins. Proline 36-43 peptidylprolyl isomerase A Homo sapiens 101-105 22185200-11 2011 The fact that this is the first non-proline containing binding motif of any protein found to bind to CypA, changes the view on how CypA is able to interact with other proteins. Proline 36-43 peptidylprolyl isomerase A Homo sapiens 131-135 20886100-6 2010 Engineering the mutations into wild-type HCV fully recapitulated the CyPA-independent and CsA-resistant phenotype and four putative proline substrates of CyPA were mapped to the vicinity of the DY motif. Proline 132-139 peptidylprolyl isomerase A Homo sapiens 154-158 21994697-3 2010 The major proline substrates are located in domain II of NS5A, centered around a "DY" dipeptide motif that regulates CyPA dependence and CsA resistance. Proline 10-17 peptidylprolyl isomerase A Homo sapiens 117-121 19380579-9 2009 We then mutated residues that reside in the hydrophobic pocket of CypA where proline-containing peptide substrates and cyclosporine A bind and that are vital for the enzymatic or the hydrophobic pocket binding activity of CypA. Proline 77-84 peptidylprolyl isomerase A Homo sapiens 66-70 19380579-9 2009 We then mutated residues that reside in the hydrophobic pocket of CypA where proline-containing peptide substrates and cyclosporine A bind and that are vital for the enzymatic or the hydrophobic pocket binding activity of CypA. Proline 77-84 peptidylprolyl isomerase A Homo sapiens 222-226 18333624-1 2008 A recombinant cyclophilin A (CypA) mutant, which carries a serine instead of proline at sequence 16, was prepared for structural and functional assessment for human CypA. Proline 77-84 peptidylprolyl isomerase A Homo sapiens 14-27 19297321-6 2009 NMR heteronuclear exchange spectroscopy yielded direct evidence that many proline residues in NS5A-D2 form a valid substrate for the enzymatic peptidyl-prolyl cis/trans isomerase (PPIase) activity of CypA and CypB. Proline 74-81 peptidylprolyl isomerase A Homo sapiens 200-204 15671024-5 2005 Peptide binding studies demonstrated specific interaction between CypA and the proline-containing peptide from the CD147 transmembrane domain. Proline 79-86 peptidylprolyl isomerase A Homo sapiens 66-70 15671024-6 2005 Mutation of this proline residue reduced binding of CD147-derived peptides to CypA and also diminished transport of CD147 to the plasma membrane without reducing the total level of CD147 expression. Proline 17-24 peptidylprolyl isomerase A Homo sapiens 78-82 12730686-2 2003 They possess both sequence-specific binding and proline cis-trans isomerase activities, as exemplified by the interaction between cyclophilin A (CypA) and the HIV-1 CA protein. Proline 48-55 peptidylprolyl isomerase A Homo sapiens 130-143 12730686-2 2003 They possess both sequence-specific binding and proline cis-trans isomerase activities, as exemplified by the interaction between cyclophilin A (CypA) and the HIV-1 CA protein. Proline 48-55 peptidylprolyl isomerase A Homo sapiens 145-149 12730686-3 2003 Here, we report crystal structures of CypA in complex with HIV-1 CA protein variants that bind preferentially with the substrate proline residue in either the cis or the trans conformation. Proline 129-136 peptidylprolyl isomerase A Homo sapiens 38-42 12730686-5 2003 CypA Arg55 guanidinium group probably facilitates catalysis by anchoring the substrate proline oxygen and stabilizing sp3 hybridization of the proline nitrogen in the transition state. Proline 87-94 peptidylprolyl isomerase A Homo sapiens 0-4 12730686-5 2003 CypA Arg55 guanidinium group probably facilitates catalysis by anchoring the substrate proline oxygen and stabilizing sp3 hybridization of the proline nitrogen in the transition state. Proline 143-150 peptidylprolyl isomerase A Homo sapiens 0-4 12009870-10 2002 Sequence analysis of the Cyp A binding regions revealed that the proline-rich motif, which is responsible for Cyp A incorporation, was conserved in all four isolates, while some sequence variations were detected in other positions close to this region. Proline 65-72 peptidylprolyl isomerase A Homo sapiens 25-30 12009870-10 2002 Sequence analysis of the Cyp A binding regions revealed that the proline-rich motif, which is responsible for Cyp A incorporation, was conserved in all four isolates, while some sequence variations were detected in other positions close to this region. Proline 65-72 peptidylprolyl isomerase A Homo sapiens 110-115 17038183-5 2006 Mutagenesis of FIV CA showed that an amino acid that is in a homologous position to the proline at amino acid 90 of HIV-1 CA is essential for FIV interactions with CypA. Proline 88-95 peptidylprolyl isomerase A Homo sapiens 164-168 16571786-4 2006 We find that Vpr coimmunoprecipitates with CypA and that this interaction is disrupted by substitution of proline-35 of Vpr as well as incubation with the CypA inhibitor cyclosporine A (CsA). Proline 106-113 peptidylprolyl isomerase A Homo sapiens 43-47 16571786-4 2006 We find that Vpr coimmunoprecipitates with CypA and that this interaction is disrupted by substitution of proline-35 of Vpr as well as incubation with the CypA inhibitor cyclosporine A (CsA). Proline 106-113 peptidylprolyl isomerase A Homo sapiens 155-159 15229879-9 2004 The results show that CA(N) residues His87-Ala-Gly-Pro-Ile-Ala92 form the majority of the interactions with CypA residues. Proline 51-54 peptidylprolyl isomerase A Homo sapiens 108-112 15147195-1 2004 The prolyl isomerase cyclophilin A (CypA) is required for efficient HIV-1 replication and is incorporated into virions through a binding interaction at the Gly-Pro(222) bond located within the capsid domain of the HIV-1 Gag precursor polyprotein (Pr(gag)). Proline 160-163 peptidylprolyl isomerase A Homo sapiens 36-40 15147195-3 2004 To address the proposal that CypA interacts with Gly-Pro sequences in the C-terminal domain of a mature capsid, the interaction between CypA and the natively folded, full-length capsid protein (CA(FL)) has been investigated here using nuclear magnetic resonance spectroscopy. Proline 53-56 peptidylprolyl isomerase A Homo sapiens 29-33 11929983-4 2002 We show here, using NMR exchange spectroscopy, that CypA does not only bind to CA(N) but also catalyzes efficiently the cis/trans isomerization of the Gly-89-Pro-90 peptide bond. Proline 158-161 peptidylprolyl isomerase A Homo sapiens 52-56