1ihm
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CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID
OverviewOverview
Norwalk virus, a noncultivatable human calicivirus, is the major cause of, epidemic gastroenteritis in humans. The first x-ray structure of a, calicivirus capsid, which consists of 180 copies of a single protein, has, been determined by phase extension from a low-resolution electron, microscopy structure. The capsid protein has a protruding (P) domain, connected by a flexible hinge to a shell (S) domain that has a classical, eight-stranded beta-sandwich motif. The structure of the P domain is, unlike that of any other viral protein with a subdomain exhibiting a fold, similar to that of the second domain in the eukaryotic translation, elongation factor-Tu. This subdomain, located at the exterior of the, capsid, has the largest sequence variation among Norwalk-like human, caliciviruses and is likely to contain the determinants of strain, specificity and cell binding.
About this StructureAbout this Structure
1IHM is a Single protein structure of sequence from Norwalk virus. Full crystallographic information is available from OCA.
ReferenceReference
X-ray crystallographic structure of the Norwalk virus capsid., Prasad BV, Hardy ME, Dokland T, Bella J, Rossmann MG, Estes MK, Science. 1999 Oct 8;286(5438):287-90. PMID:10514371
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