4DGE

TRIMCyp cyclophilin domain from Macaca mulatta: H70C mutant, HIV-1 CA(O-loop) complex

4DGE の概要

• エントリーDOI: 10.2210/pdb4dge/pdb
• 関連するPDBエントリー: 4DGA 4DGB 4DGC 4DGD
• 分子名称: TRIMCyp, capsid protein (3 entities in total)
• 機能のキーワード: anti-viral protein, isomerase-viral protein complex, isomerase/viral protein
• 由来する生物種: Macaca mulatta (rhesus macaque); 詳細
• 細胞内の位置: Capsid protein p24: Virion (By similarity). Matrix protein p17: Virion (By similarity). Nucleocapsid protein p7: Virion (By similarity): Q72497
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68322.10

構造登録者

Caines, M.E.C.,Bichel, K.,Price, A.J.,McEwan, W.A.,James, L.C. (登録日: 2012-01-25, 公開日: 2012-02-08, 最終更新日: 2024-11-27)

主引用文献

Caines, M.E.,Bichel, K.,Price, A.J.,McEwan, W.A.,Towers, G.J.,Willett, B.J.,Freund, S.M.,James, L.C.
Diverse HIV viruses are targeted by a conformationally dynamic antiviral.
Nat.Struct.Mol.Biol., 19:411-416, 2012

PubMed Abstract: Rhesus macaque TRIMCyp (RhTC) is a potent primate antiviral host protein that inhibits the replication of diverse HIV viruses. Here we show that it has acquired the ability to target multiple viruses by evolving an active site that interconverts between multiple conformations. Mutations that have relieved active site constraints allow RhTC to dynamically sample conformational space, including radically different conformers that target both HIV-1 and HIV-2 viruses. Introduction of a reversible constraint into RhTC allows specificity to be switched between a single conformation specific for HIV-1 and a dynamic ensemble that targets multiple viruses. These results show that conformational diversity can be used to expand the target diversity of innate immune receptors by supplementing their limited genetic variability with variability in protein structure.

PubMed: 22407016
DOI: 10.1038/nsmb.2253

実験手法

X-RAY DIFFRACTION (2.2 Å)