3GV2

X-ray Structure of Hexameric HIV-1 CA

3GV2 の概要

• エントリーDOI: 10.2210/pdb3gv2/pdb
• 関連するPDBエントリー: 3H47 3H4E
• 分子名称: Capsid protein p24,Carbon dioxide-concentrating mechanism protein CcmK homolog 4 (1 entity in total)
• 機能のキーワード: hexameric retroviral capsid, viral protein
• 由来する生物種: Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 223864.03

構造登録者

Kelly, B.N. (登録日: 2009-03-30, 公開日: 2009-06-23, 最終更新日: 2024-02-21)

主引用文献

Pornillos, O.,Ganser-Pornillos, B.K.,Kelly, B.N.,Hua, Y.,Whitby, F.G.,Stout, C.D.,Sundquist, W.I.,Hill, C.P.,Yeager, M.
X-ray structures of the hexameric building block of the HIV capsid.
Cell(Cambridge,Mass.), 137:1282-1292, 2009

PubMed Abstract: The mature capsids of HIV and other retroviruses organize and package the viral genome and its associated enzymes for delivery into host cells. The HIV capsid is a fullerene cone: a variably curved, closed shell composed of approximately 250 hexamers and exactly 12 pentamers of the viral CA protein. We devised methods for isolating soluble, assembly-competent CA hexamers and derived four crystallographically independent models that define the structure of this capsid assembly unit at atomic resolution. A ring of six CA N-terminal domains form an apparently rigid core, surrounded by an outer ring of C-terminal domains. Mobility of the outer ring appears to be an underlying mechanism for generating the variably curved lattice in authentic capsids. Hexamer-stabilizing interfaces are highly hydrated, and this property may be key to the formation of quasi-equivalent interactions within hexamers and pentamers. The structures also clarify the molecular basis for capsid assembly inhibition and should facilitate structure-based drug design strategies.

PubMed: 19523676
DOI: 10.1016/j.cell.2009.04.063

実験手法

X-RAY DIFFRACTION (7 Å)