2b4h
From Proteopedia
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Crystal Structure of the Rhesus Rotavirus VP5 Antigen Domain Dimer
Overview
The spike protein VP4 is a key component of the membrane penetration, apparatus of rotavirus, a nonenveloped virus that causes childhood, gastroenteritis. Trypsin cleavage of VP4 produces a fragment, VP5*, with a, potential membrane interaction region, and primes rotavirus for cell, entry. During entry, the part of VP5* that protrudes from the virus folds, back on itself and reorganizes from a local dimer to a trimer. Here, we, report that a globular domain of VP5*, the VP5* antigen domain, is an, autonomously folding unit that alternatively forms well-ordered dimers and, trimers. Because the domain contains heterotypic neutralizing epitopes and, is soluble when expressed directly, it is a promising potential subunit, vaccine component. X-ray crystal structures show that the dimer resembles, the spike body on trypsin-primed virions, and the trimer resembles the, folded-back form of the spike. The same structural elements pack, differently to form key intermolecular contacts in both oligomers. The, intrinsic molecular property of alternatively forming dimers and trimers, facilitates the VP5* reorganization, which is thought to mediate membrane, penetration during cell entry.
About this Structure
2B4H is a Single protein structure of sequence from Rhesus rotavirus with and as ligands. Full crystallographic information is available from OCA.
Reference
Alternative intermolecular contacts underlie the rotavirus VP5* two- to three-fold rearrangement., Yoder JD, Dormitzer PR, EMBO J. 2006 Apr 5;25(7):1559-68. Epub 2006 Mar 2. PMID:16511559
Page seeded by OCA on Tue Jan 29 18:16:33 2008
