4XFX

Structure of the native full-length HIV-1 capsid protein

4XFX の概要

• エントリーDOI: 10.2210/pdb4xfx/pdb
• 関連するPDBエントリー: 4XFY 4XFZ
• 分子名称: HIV-1 capsid protein, IODIDE ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: capsid protein, native, viral protein
• 由来する生物種: Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26589.66

構造登録者

Gres, A.T.,Kirby, K.A.,Sarafianos, S.G. (登録日: 2014-12-29, 公開日: 2015-06-10, 最終更新日: 2024-11-20)

主引用文献

Gres, A.T.,Kirby, K.A.,KewalRamani, V.N.,Tanner, J.J.,Pornillos, O.,Sarafianos, S.G.
STRUCTURAL VIROLOGY. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability.
Science, 349:99-103, 2015

PubMed Abstract: The detailed molecular interactions between native HIV-1 capsid protein (CA) hexamers that shield the viral genome and proteins have been elusive. We report crystal structures describing interactions between CA monomers related by sixfold symmetry within hexamers (intrahexamer) and threefold and twofold symmetry between neighboring hexamers (interhexamer). The structures describe how CA builds hexagonal lattices, the foundation of mature capsids. Lattice structure depends on an adaptable hydration layer modulating interactions among CA molecules. Disruption of this layer alters interhexamer interfaces, highlighting an inherent structural variability. A CA-targeting antiviral affects capsid stability by binding across CA molecules and subtly altering interhexamer interfaces remote to the ligand-binding site. Inherent structural plasticity, hydration layer rearrangement, and effector binding affect capsid stability and have functional implications for the retroviral life cycle.

PubMed: 26044298
DOI: 10.1126/science.aaa5936

実験手法

X-RAY DIFFRACTION (2.43 Å)