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X-ray Crystallographic Structure of the Norwalk Virus Capsid

Prasad, B. V. V., Hardy, Michele E., Dokland, Terje, Bella, Jordi, Rossmann, Michael G., Estes, Mary K.·1999·Science

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.

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Metadata

Authors
Prasad, B. V. V., Hardy, M. E., Dokland, T., Bella, J., Rossmann, M. G., & Estes, M. K.
Venue
Science
Published
1999-10-08
Volume
286
Issue
5438
Pages
287-290
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2130788389
Cited by
946
References
2
FWCI
11.18
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: X-ray Crystallographic Structure of the Norwalk Virus Capsid. https://app.cochat.ai/papers/10.1126/science.286.5438.287
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Prasad, B. V. V., Hardy, M. E., Dokland, T., Bella, J., Rossmann, M. G., & Estes, M. K. (1999). X-ray Crystallographic Structure of the Norwalk Virus Capsid. Science. https://doi.org/10.1126/science.286.5438.287

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