2ONT

A swapped dimer of the HIV-1 capsid C-terminal domain

2ONT の概要

• エントリーDOI: 10.2210/pdb2ont/pdb
• 分子名称: Capsid protein p24 (2 entities in total)
• 機能のキーワード: hiv; capsid; gag; domain swap, viral protein
• 由来する生物種: Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)
• 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): P12497
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8540.74

構造登録者

Ivanov, D.,Tsodikov, O.V.,Kasanov, J.,Ellenberger, T.,Wagner, G.,Collins, T. (登録日: 2007-01-24, 公開日: 2007-02-20, 最終更新日: 2023-08-30)

主引用文献

Ivanov, D.,Tsodikov, O.V.,Kasanov, J.,Ellenberger, T.,Wagner, G.,Collins, T.
Domain-swapped dimerization of the HIV-1 capsid C-terminal domain
Proc.Natl.Acad.Sci.Usa, 104:4353-4358, 2007

PubMed Abstract: Assembly of the HIV and other retroviruses is primarily driven by the oligomerization of the Gag polyprotein, the major viral structural protein capable of forming virus-like particles even in the absence of all other virally encoded components. Several critical determinants of Gag oligomerization are located in the C-terminal domain of the capsid protein (CA-CTD), which encompasses the most conserved segment in the highly variable Gag protein called the major homology region (MHR). The CA-CTD is thought to function as a dimerization module, although the existing model of CA-CTD dimerization does not readily explain why the conserved residues of the MHR are essential for retroviral assembly. Here we describe an x-ray structure of a distinct domain-swapped variant of the HIV-1 CA-CTD dimer stabilized by a single amino acid deletion. In the domain-swapped structure, the MHR-containing segment forms a major part of the dimerization interface, providing a structural mechanism for the enigmatic function of the MHR in HIV assembly. Our observations suggest that swapping of the MHR segments of adjacent Gag molecules may be a critical intermediate in retroviral assembly.

PubMed: 17360528
DOI: 10.1073/pnas.0609477104

実験手法

X-RAY DIFFRACTION (2.4 Å)