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X-ray Crystallographic Structure of the Norwalk Virus Capsid

Science  08 Oct 1999:
Vol. 286, Issue 5438, pp. 287-290
DOI: 10.1126/science.286.5438.287

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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 β-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.

  • * To whom correspondence should be addressed. E-mail: vprasad{at}bcm.tmc.edu

  • Present address: Veterinary Molecular Biology, Montana State University, Bozeman, MT 59717, USA.

  • Present address: Institute of Molecular Agrobiology, National University of Singapore, Singapore 117604.

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