2j6j
From Proteopedia
PREFUSION FORM OF THE VESICULAR STOMATITIS VIRUS GLYCOPROTEIN G ECTODOMAIN
Structural highlights
Function[GLYCO_VSIVA] Attaches the virus to host LDL receptors, inducing clathrin-dependent endocytosis of the virion.[1] [2] In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and endosomal membrane.[3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlycoprotein G of the vesicular stomatitis virus triggers membrane fusion via a low pH-induced structural rearrangement. Despite the equilibrium between the pre- and postfusion states, the structure of the prefusion form, determined to 3.0 angstrom resolution, shows that the fusogenic transition entails an extensive structural reorganization of G. Comparison with the structure of the postfusion form suggests a pathway for the conformational change. In the prefusion form, G has the shape of a tripod with the fusion loops exposed, which point toward the viral membrane, and with the antigenic sites located at the distal end of the molecule. A large number of G glycoproteins, perhaps organized as in the crystals, act cooperatively to induce membrane merging. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G.,Roche S, Rey FA, Gaudin Y, Bressanelli S Science. 2007 Feb 9;315(5813):843-8. PMID:17289996[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
