1AWS

SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)

1AWS の概要

• エントリーDOI: 10.2210/pdb1aws/pdb
• 分子名称: CYCLOPHILIN A, PEPTIDE FROM THE HIV-1 CAPSID PROTEIN (3 entities in total)
• 機能のキーワード: complex (isomerase-peptide), cyclophilin a, hiv-1 capsid, pseudo-symmetry, complex (isomerase-peptide) complex, complex (isomerase/peptide)
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18658.53

構造登録者

Vajdos, F.F. (登録日: 1997-10-04, 公開日: 1998-03-18, 最終更新日: 2024-10-16)

主引用文献

Vajdos, F.F.,Yoo, S.,Houseweart, M.,Sundquist, W.I.,Hill, C.P.
Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.
Protein Sci., 6:2297-2307, 1997

PubMed Abstract: 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.

PubMed: 9385632

実験手法

X-RAY DIFFRACTION (2.55 Å)