1JEK

Visna TM CORE STRUCTURE

1JEK の概要

• エントリーDOI: 10.2210/pdb1jek/pdb
• 分子名称: ENV POLYPROTEIN (3 entities in total)
• 機能のキーワード: envelope glycoprotein, retrovirus, hiv, siv, gp41, viral protein
• 細胞内の位置: Transmembrane protein: Virion membrane; Single-pass type I membrane protein (By similarity). Surface protein: Virion membrane; Peripheral membrane protein (By similarity): P35954 P35954
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8463.52

構造登録者

Malashkevich, V.N.,Singh, M.,Kim, P.S. (登録日: 2001-06-18, 公開日: 2001-07-25, 最終更新日: 2024-10-30)

主引用文献

Malashkevich, V.N.,Singh, M.,Kim, P.S.
The trimer-of-hairpins motif in membrane fusion: Visna virus.
Proc.Natl.Acad.Sci.USA, 98:8502-8506, 2001

PubMed Abstract: Structural studies of viral membrane fusion proteins suggest that a "trimer-of-hairpins" motif plays a critical role in the membrane fusion process of many enveloped viruses. In this motif, a coiled coil (formed by homotrimeric association of the N-terminal regions of the protein) is surrounded by three C-terminal regions that pack against the coiled coil in an oblique antiparallel manner. The resulting trimer-of-hairpins structure serves to bring the viral and cellular membranes together for fusion. learncoil-vmf, a computational program developed to recognize coiled coil-like regions that form the trimer-of-hairpins motif, predicts these regions in the membrane fusion protein of the Visna virus. Peptides corresponding to the computationally identified sequences were synthesized, and the soluble core of the Visna membrane fusion protein was reconstituted in solution. Its crystal structure at 1.5-A resolution demonstrates that a trimer-of-hairpins structure is formed. Remarkably, despite less than 23% sequence identity, the ectodomains in Visna and HIV-1 envelope glycoproteins show detailed structural conservation, especially within the area of a hydrophobic pocket in the central coiled coil currently being targeted for the development of new anti-HIV drugs.

PubMed: 11447278
DOI: 10.1073/pnas.151254798

実験手法

X-RAY DIFFRACTION (1.5 Å)