

@article {5551,
	title = {{X-ray crystallographic structure of the Norwalk virus capsid.}},
	journal = {Science (New York, N.Y.)},
	volume = {286},
	number = {5438},
	year = {1999},
	pages = {287{\textendash}290},
	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.},
	isbn = {0036-8075 (Print)$\backslash$r0036-8075 (Linking)},
	issn = {0036-8075},
	doi = {10.1126/science.286.5438.287},
	author = {Prasad, B V and Hardy, M E and Dokland, T and Bella, J and Rossmann, M G and Estes, M K}
}
