2cmz

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:37:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:50:20 2008''

Revision as of 14:50, 21 February 2008


2cmz, resolution 2.40Å

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CRYSTAL STRUCTURE OF VSV-INDIANA (MUDD-SUMMERS STRAIN) GLYCOPROTEIN UNDER ITS ACIDIC CONFORMATION

Overview

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.

About this Structure

2CMZ is a Single protein structure of sequence from Vesicular stomatitis indiana virus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

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

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