Download MendeleyX-ray crystallographic structure of the Norwalk virus capsid
Prasad, B.V., Hardy, M.E., Dokland, T., Bella, J., Rossmann, M.G., Estes, M.K.(1999) Science 286: 287-290
- PubMed: 10514371
- DOI: https://doi.org/10.1126/science.286.5438.287
- Primary Citation of Related Structures:
1IHM - PubMed Abstract:
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.
Organizational Affiliation:
Verna and Marrs Mclean Department of Biochemistry, Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, USA. [email protected]
