The atomic structure of the bluetongue virus core.
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.
Department of Biochemistry, University of Oxford, UK.
J M
JM
Grimes
J N
JN
Burroughs
P
P
Gouet
J M
JM
Diprose
R
R
Malby
S
S
Ziéntara
P P
PP
Mertens
D I
DI
Stuart
D000595:Amino Acid Sequence; D001820:Bluetongue virus / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D012367:RNA, Viral / Q000737:chemistry; D014758:Viral Core Proteins / Q000737:chemistry* / Q000378:metabolism
D012367:RNA, Viral; C074954:VP3 protein, Bluetongue virus; D014758:Viral Core Proteins; C066862:VP7 protein, orbivirus