1ihm
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 Page seeded by OCA on Fri May 2 20:00:35 2008