Crystal Structure of the Low-pH Form of the Vesicular Stomatitis Virus Glycoprotein G
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- 14 July 2006
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 313 (5784) , 187-191
- https://doi.org/10.1126/science.1127683
Abstract
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.Keywords
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