3MKO

Crystal Structure of the Lymphocytic Choriomeningitis Virus Membrane Fusion Glycoprotein GP2 in its Postfusion Conformation

3MKO の概要

• エントリーDOI: 10.2210/pdb3mko/pdb
• 分子名称: Glycoprotein C, (4S)-2-METHYL-2,4-PENTANEDIOL, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: trimeric coiled-coil, viral protein
• 由来する生物種: Lymphocytic choriomeningitis virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16781.22

構造登録者

Igonet, S.,Vaney, M.C.,Rey, F.A. (登録日: 2010-04-15, 公開日: 2011-04-20, 最終更新日: 2024-10-30)

主引用文献

Igonet, S.,Vaney, M.C.,Vonhrein, C.,Bricogne, G.,Stura, E.A.,Hengartner, H.,Eschli, B.,Rey, F.A.
X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation
Proc.Natl.Acad.Sci.USA, 108:19967-19972, 2011

PubMed Abstract: Arenaviruses are important agents of zoonotic disease worldwide. The virions expose a tripartite envelope glycoprotein complex at their surface, formed by the glycoprotein subunits GP1, GP2 and the stable signal peptide. This complex is responsible for binding to target cells and for the subsequent fusion of viral and host-cell membranes for entry. During this process, the acidic environment of the endosome triggers a fusogenic conformational change in the transmembrane GP2 subunit of the complex. We report here the crystal structure of the recombinant GP2 ectodomain of the lymphocytic choriomeningitis virus, the arenavirus type species, at 1.8-Å resolution. The structure shows the characteristic trimeric coiled coil present in class I viral fusion proteins, with a central stutter that allows a close structural alignment with most of the available structures of class I and III viral fusion proteins. The structure further shows a number of intrachain salt bridges stabilizing the postfusion hairpin conformation, one of which involves an aspartic acid that appears released from a critical interaction with the stable signal peptide upon low pH activation.

PubMed: 22123988
DOI: 10.1073/pnas.1108910108

実験手法

X-RAY DIFFRACTION (1.8 Å)