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| [[Image:1awq.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1awq| PDB=1awq | SCENE= }} | | {{STRUCTURE_1awq| PDB=1awq | SCENE= }} |
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| '''CYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)'''
| | ===CYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)=== |
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| ==Overview==
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| The cellular protein, cyclophilin A (CypA), is incorporated into the virion of the type 1 human immunodeficiency virus (HIV-1) via a direct interaction with the capsid domain of the viral Gag polyprotein. 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. 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. We also report the crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_9385632}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9385632 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9385632}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hiv-1 capsid]] | | [[Category: Hiv-1 capsid]] |
| [[Category: Pseudo-symmetry]] | | [[Category: Pseudo-symmetry]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:47:03 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:45:17 2008'' |
