2GON

Xray Structure of Gag133-278

2GON の概要

• エントリーDOI: 10.2210/pdb2gon/pdb
• 関連するPDBエントリー: 2GOL
• 分子名称: Capsid protein p24 (CA), CITRATE ANION (3 entities in total)
• 機能のキーワード: hiv-1 ca, capsid, beta hairpin, gag, immature, mature, viral protein
• 由来する生物種: Human immunodeficiency virus 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): P12497
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66929.28

構造登録者

Kelly, B.N. (登録日: 2006-04-13, 公開日: 2006-09-26, 最終更新日: 2024-11-20)

主引用文献

Kelly, B.N.,Howard, B.R.,Wang, H.,Robinson, H.,Sundquist, W.I.,Hill, C.P.
Implications for Viral Capsid Assembly from Crystal Structures of HIV-1 Gag 1-278 and CAN 133-278.
Biochemistry, 45:11257-11266, 2006

PubMed Abstract: Gag, the major structural protein of retroviruses such as HIV-1, comprises a series of domains connected by flexible linkers. These domains drive viral assembly by mediating multiple interactions between adjacent Gag molecules and by binding to viral genomic RNA and host cell membranes. Upon viral budding, Gag is processed by the viral protease to liberate distinct domains as separate proteins. The first two regions of Gag are MA, a membrane-binding module, and CA, which is a two-domain protein that makes important Gag-Gag interactions, forms the cone-shaped outer shell of the core (the capsid) in the mature HIV-1 particle, and makes an important interaction with the cellular protein cyclophilin A (CypA). Here, we report crystal structures of the mature CA N-terminal domain (CA(N)(133-278)) and a MA-CA(N) fusion (Gag(1-278)) at resolutions/R(free) values of 1.9 A/25.7% and 2.2 A/25.8%, respectively. Consistent with earlier studies, a comparison of these structures indicates that processing at the MA-CA junction causes CA to adopt an N-terminal beta-hairpin conformation that seems to be required for capsid morphology and viral infectivity. In contrast with an NMR study (Tang, C., et al. (2002) Nat. Struct. Biol. 9, 537-543), structural overlap reveals only small relative displacements for helix 6, which is located between the beta-hairpin and the CypA-binding loop. These observations argue against the proposal that CypA binding is coupled with beta-hairpin formation and support an earlier surface plasmon resonance study (Yoo, S., et al. (1997) J. Mol. Biol. 269, 780-795), which concluded that beta-hairpin formation and CypA-binding are energetically independent events.

PubMed: 16981686
DOI: 10.1021/bi060927x

実験手法

X-RAY DIFFRACTION (1.9 Å)