1M9C

X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.

1M9C の概要

• エントリーDOI: 10.2210/pdb1m9c/pdb
• 関連するPDBエントリー: 1AK4 1M96 1M9D 1M9E 1M9F 1M9X 1M9Y
• 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, isomerase-viral protein complex, isomerase/viral protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P62937; Matrix protein p17: Virion (By similarity): Q72497
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68482.15

構造登録者

Howard, B.R.,Vajdos, F.F.,Li, S.,Sundquist, W.I.,Hill, C.P. (登録日: 2002-07-28, 公開日: 2003-05-27, 最終更新日: 2024-02-14)

主引用文献

Howard, B.R.,Vajdos, F.F.,Li, S.,Sundquist, W.I.,Hill, C.P.
Structural insights into the catalytic mechanism of cyclophilin A
Nat.Struct.Biol., 10:475-481, 2003

PubMed Abstract: Cyclophilins constitute a ubiquitous protein family whose functions include protein folding, transport and signaling. They possess both sequence-specific binding and proline cis-trans isomerase activities, as exemplified by the interaction between cyclophilin A (CypA) and the HIV-1 CA protein. Here, we report crystal structures of CypA in complex with HIV-1 CA protein variants that bind preferentially with the substrate proline residue in either the cis or the trans conformation. Cis- and trans-Pro substrates are accommodated within the enzyme active site by rearrangement of their N-terminal residues and with minimal distortions in the path of the main chain. CypA Arg55 guanidinium group probably facilitates catalysis by anchoring the substrate proline oxygen and stabilizing sp3 hybridization of the proline nitrogen in the transition state.

PubMed: 12730686
DOI: 10.1038/nsb927

実験手法

X-RAY DIFFRACTION (2 Å)