2gh8
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gh8 OCA], [http://www.ebi.ac.uk/pdbsum/2gh8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gh8 RCSB]</span> | ||
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[[Category: vesivirus]] | [[Category: vesivirus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:16:38 2008'' |
Revision as of 00:16, 31 March 2008
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| , resolution 3.20Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray structure of a native calicivirus
Overview
Caliciviruses, grouped into four genera, are important human and veterinary pathogens with a potential for zoonosis. In these viruses, capsid-related functions such as assembly, antigenicity, and receptor interactions are predominantly encoded in a single protein that forms an icosahedral capsid. Understanding of the immunologic functions and pathogenesis of human caliciviruses in the Norovirus and Sapovirus genera is hampered by the lack of a cell culture system or animal models. Much of our understanding of these viruses, including the structure, has depended on recombinant capsids. Here we report the atomic structure of a native calicivirus from the Vesivirus genus that exhibits a broad host range possibly including humans and map immunological function onto a calicivirus structure. The vesivirus structure, despite a similar architectural design as seen in the recombinant norovirus capsid, exhibits novel features and indicates how the unique modular organization of the capsid protein with interdomain flexibility, similar to an antibody structure with a hinge and an elbow, integrates capsid-related functions and facilitates strain diversity in caliciviruses. The internally located N-terminal arm participates in a novel network of interactions through domain swapping to assist the assembly of the shell domain into an icosahedral scaffold, from which the protruding domain emanates. Neutralization epitopes localize to three hypervariable loops in the distal portion of the protruding domain surrounding a region that exhibits host-specific conservation. These observations suggest a mechanism for antigenic diversity and host specificity in caliciviruses and provide a structural framework for vaccine development.
About this Structure
2GH8 is a Single protein structure of sequence from San miguel sea lion virus 4. Full crystallographic information is available from OCA.
Reference
X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity., Chen R, Neill JD, Estes MK, Prasad BV, Proc Natl Acad Sci U S A. 2006 May 23;103(21):8048-53. Epub 2006 May 15. PMID:16702551
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