PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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. Dipeptides 86-95 peptidylprolyl isomerase A Homo sapiens 117-121 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. Dipeptides 67-76 peptidylprolyl isomerase A Homo sapiens 180-184 9223641-6 1997 The energetic contributions to CypA binding were quantified for each residue in this loop, and the results demonstrate that the Gly89-Pro90 dipeptide is the primary cyclophilin A recognition motif, with Pro85, Val86, His87, Ala88, and Pro93 also making energetically favorable contacts. Dipeptides 140-149 peptidylprolyl isomerase A Homo sapiens 31-35 9223641-6 1997 The energetic contributions to CypA binding were quantified for each residue in this loop, and the results demonstrate that the Gly89-Pro90 dipeptide is the primary cyclophilin A recognition motif, with Pro85, Val86, His87, Ala88, and Pro93 also making energetically favorable contacts. Dipeptides 140-149 peptidylprolyl isomerase A Homo sapiens 165-178 8075981-6 1994 Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation. Dipeptides 165-174 peptidylprolyl isomerase A Homo sapiens 82-86 8075981-6 1994 Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation. Dipeptides 165-174 peptidylprolyl isomerase A Homo sapiens 91-95 8075981-6 1994 Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation. Dipeptides 165-174 peptidylprolyl isomerase A Homo sapiens 91-95