5UP4

Structure of the HIV-1 Capsid Protein and spacer peptide 1 by Cryo-EM

5UP4 の概要

• エントリーDOI: 10.2210/pdb5up4/pdb
• EMDBエントリー: 8582
• 分子名称: HIV-1 Capsid Protein and spacer peptide 1 (1 entity in total)
• 機能のキーワード: hiv-1, spacer peptide 1, capsid protein, cryoem, helical assembly, reconstruction, virus
• 由来する生物種: Human immunodeficiency virus 1
• 細胞内の位置: Host cytoplasm . Host nucleus . Matrix protein p17: Virion . Virion : B6DRA0
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 443776.82

構造登録者

Perilla, J.R.,Schirra, R.,Zhang, P.,Schulten, K. (登録日: 2017-02-01, 公開日: 2017-12-06, 最終更新日: 2024-11-20)

主引用文献

Wang, M.,Quinn, C.M.,Perilla, J.R.,Zhang, H.,Shirra, R.,Hou, G.,Byeon, I.J.,Suiter, C.L.,Ablan, S.,Urano, E.,Nitz, T.J.,Aiken, C.,Freed, E.O.,Zhang, P.,Schulten, K.,Gronenborn, A.M.,Polenova, T.
Quenching protein dynamics interferes with HIV capsid maturation.
Nat Commun, 8:1779-1779, 2017

PubMed Abstract: Maturation of HIV-1 particles encompasses a complex morphological transformation of Gag via an orchestrated series of proteolytic cleavage events. A longstanding question concerns the structure of the C-terminal region of CA and the peptide SP1 (CA-SP1), which represents an intermediate during maturation of the HIV-1 virus. By integrating NMR, cryo-EM, and molecular dynamics simulations, we show that in CA-SP1 tubes assembled in vitro, which represent the features of an intermediate assembly state during maturation, the SP1 peptide exists in a dynamic helix-coil equilibrium, and that the addition of the maturation inhibitors Bevirimat and DFH-055 causes stabilization of a helical form of SP1. Moreover, the maturation-arresting SP1 mutation T8I also induces helical structure in SP1 and further global dynamical and conformational changes in CA. Overall, our results show that dynamics of CA and SP1 are critical for orderly HIV-1 maturation and that small molecules can inhibit maturation by perturbing molecular motions.

PubMed: 29176596
DOI: 10.1038/s41467-017-01856-y

実験手法

ELECTRON MICROSCOPY (9 Å)