1ihm | pdb_00001ihm

CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID

spinqualitylabelsall models 1ihm, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ihm is a 3 chain structure with sequence from Norwalk virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum 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 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat protein

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