1w9z
From Proteopedia
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STRUCTURE OF BANNAVIRUS VP9
Overview
Banna virus (BAV: genus Seadornavirus, family Reoviridae) has a, double-shelled morphology similar to rotavirus and bluetongue virus. The, structure of BAV outer-capsid protein VP9 was determined by X-ray, crystallography at 2.6 A resolution, revealing a trimeric molecule, held, together by an N-terminal helical bundle, reminiscent of coiled-coil, structures found in fusion-active proteins such as HIV gp41. The major, domain of VP9 contains stacked beta sheets with marked structural, similarities to the receptor binding protein VP8 of rotavirus. Anti-VP9, antibodies neutralize viral infectivity, and, remarkably, pretreatment of, cells with trimeric VP9 increased viral infectivity, indicating that VP9, is involved in virus attachment to cell surface and subsequent, internalization. Sequence similarities were also detected between BAV VP10, and VP5 portion of rotavirus VP4, suggesting that the receptor binding and, internalization apparatus, which is a single gene product activated by, proteoloysis in rotavirus, is the product of two separate genome segments, in BAV.
About this Structure
1W9Z is a Single protein structure of sequence from Banna virus. Full crystallographic information is available from OCA.
Reference
The structure and function of the outer coat protein VP9 of Banna virus., Mohd Jaafar F, Attoui H, Bahar MW, Siebold C, Sutton G, Mertens PP, De Micco P, Stuart DI, Grimes JM, De Lamballerie X, Structure. 2005 Jan;13(1):17-28. PMID:15642258
Page seeded by OCA on Sat Nov 24 23:37:40 2007
