Structural highlights
Function
VGLG_VSIVM
Publication Abstract from PubMed
The vesicular stomatitis virus has an atypical membrane fusion glycoprotein (G) exhibiting a pH-dependent equilibrium between two forms at the virus surface. Membrane fusion is triggered during the transition from the high- to low-pH form. The structure of G in its low-pH form shows the classic hairpin conformation observed in all other fusion proteins in their postfusion conformation, in spite of a novel fold combining features of fusion proteins from classes I and II. The structure provides a framework for understanding the reversibility of the G conformational change. Unexpectedly, G is homologous to gB of herpesviruses, which raises important questions on viral evolution.
Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G.,Roche S, Bressanelli S, Rey FA, Gaudin Y Science. 2006 Jul 14;313(5784):187-91. PMID:16840692[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roche S, Bressanelli S, Rey FA, Gaudin Y. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science. 2006 Jul 14;313(5784):187-91. PMID:16840692 doi:313/5784/187