Structural highlights
Function
[VP3_BTV1S] The VP3 protein is one of the five proteins (with VP1, VP4, VP6 and VP7) which form the inner capsid of the virus. [VP7_BTV1S] The VP7 protein is one of the five proteins (with VP1, VP3, VP4, and VP6) which form the inner capsid of the virus.
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 PubMed
The structure of the core particle of bluetongue virus has been determined by X-ray crystallography at a resolution approaching 3.5 A. This transcriptionally active compartment, 700 A in diameter, represents the largest molecular structure determined in such detail. The atomic structure indicates how approximately 1,000 protein components self-assemble, using both the classical mechanism of quasi-equivalent contacts, which are achieved through triangulation, and a different method, which we term geometrical quasi-equivalence.
The atomic structure of the bluetongue virus core.,Grimes JM, Burroughs JN, Gouet P, Diprose JM, Malby R, Zientara S, Mertens PP, Stuart DI Nature. 1998 Oct 1;395(6701):470-8. PMID:9774103[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grimes JM, Burroughs JN, Gouet P, Diprose JM, Malby R, Zientara S, Mertens PP, Stuart DI. The atomic structure of the bluetongue virus core. Nature. 1998 Oct 1;395(6701):470-8. PMID:9774103 doi:10.1038/26694
