5i2m

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.