1AK4

HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID

1AK4 の概要

• エントリーDOI: 10.2210/pdb1ak4/pdb
• 分子名称: CYCLOPHILIN A, HIV-1 CAPSID (3 entities in total)
• 機能のキーワード: capsid, hiv-1, cyclophilin a, isomerase, rotamase complex (capsid protein-cyclosporin), viral protein-isomerase complex, viral protein/isomerase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P62937; Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68308.00

構造登録者

Hill, C.P.,Gamble, T.R.,Vajdos, F.F.,Worthylake, D.K.,Sundquist, W.I. (登録日: 1997-05-28, 公開日: 1997-10-15, 最終更新日: 2024-05-22)

主引用文献

Gamble, T.R.,Vajdos, F.F.,Yoo, S.,Worthylake, D.K.,Houseweart, M.,Sundquist, W.I.,Hill, C.P.
Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid.
Cell(Cambridge,Mass.), 87:1285-1294, 1996

PubMed Abstract: The HIV-1 capsid protein forms the conical core structure at the center of the mature virion. Capsid also binds the human peptidyl prolyl isomerase, cyclophilin A, thereby packaging the enzyme into the virion. Cyclophilin A subsequently performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection. We report the 2.36 A crystal structure of the N-terminal domain of HIV-1 capsid (residues 1-151) in complex with human cyclophilin A. A single exposed capsid loop (residues 85-93) binds in the enzyme's active site, and Pro-90 adopts an unprecedented trans conformation. The structure suggests how cyclophilin A can act as a sequence-specific binding protein and a nonspecific prolyl isomerase. In the crystal lattice, capsid molecules assemble into continuous planar strips. Side by side association of these strips may allow capsid to form the surface of the viral core. Cyclophilin A could then function by weakening the association between capsid strips, thereby promoting disassembly of the viral core.

PubMed: 8980234
DOI: 10.1016/S0092-8674(00)81823-1

実験手法

X-RAY DIFFRACTION (2.36 Å)