Pub. Date : 1997 Nov
PMID : 9385632
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | 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 | peptidylprolyl isomerase A | Homo sapiens |
| 2 | 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 | peptidylprolyl isomerase A | Homo sapiens |
| 3 | 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 | peptidylprolyl isomerase A | Homo sapiens |
| 4 | 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 | peptidylprolyl isomerase A | Homo sapiens |
| 5 | 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 | peptidylprolyl isomerase A | Homo sapiens |
| 6 | 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 | peptidylprolyl isomerase A | Homo sapiens |