2KOD

A high-resolution NMR structure of the dimeric C-terminal domain of HIV-1 CA

2KOD の概要

• エントリーDOI: 10.2210/pdb2kod/pdb
• 分子名称: HIV-1 CA C-terminal domain (1 entity in total)
• 機能のキーワード: hiv-1 capsid, c-terminal domain, viral protein
• 由来する生物種: HIV-1 M:B_HXB2R (HIV-1)
• 細胞内の位置: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P04585
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19678.63

構造登録者

Byeon, I.-J.L.,Jung, J.,Ahn, J.,concel, J.,Gronenborn, A.M. (登録日: 2009-09-18, 公開日: 2009-11-24, 最終更新日: 2024-05-01)

主引用文献

Byeon, I.J.,Meng, X.,Jung, J.,Zhao, G.,Yang, R.,Ahn, J.,Shi, J.,Concel, J.,Aiken, C.,Zhang, P.,Gronenborn, A.M.
Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function.
Cell(Cambridge,Mass.), 139:780-790, 2009

PubMed Abstract: Mature HIV-1 particles contain conical-shaped capsids that enclose the viral RNA genome and perform essential functions in the virus life cycle. Previous structural analysis of two- and three-dimensional arrays of the capsid protein (CA) hexamer revealed three interfaces. Here, we present a cryoEM study of a tubular assembly of CA and a high-resolution NMR structure of the CA C-terminal domain (CTD) dimer. In the solution dimer structure, the monomers exhibit different relative orientations compared to previous X-ray structures. The solution structure fits well into the EM density map, suggesting that the dimer interface is retained in the assembled CA. We also identified a CTD-CTD interface at the local three-fold axis in the cryoEM map and confirmed its functional importance by mutagenesis. In the tubular assembly, CA intermolecular interfaces vary slightly, accommodating the asymmetry present in tubes. This provides the necessary plasticity to allow for controlled virus capsid dis/assembly.

PubMed: 19914170
DOI: 10.1016/j.cell.2009.10.010

実験手法

SOLUTION NMR