2aen
From Proteopedia
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'''Crystal structure of the rotavirus strain DS-1 VP8* core''' | '''Crystal structure of the rotavirus strain DS-1 VP8* core''' | ||
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[[Category: Sun, Z Y.J.]] | [[Category: Sun, Z Y.J.]] | ||
[[Category: Taniguchi, K.]] | [[Category: Taniguchi, K.]] | ||
| - | [[Category: | + | [[Category: Neutralization antigen]] |
| - | [[Category: | + | [[Category: Rotavirus]] |
| - | [[Category: | + | [[Category: Spike protein]] |
| - | [[Category: | + | [[Category: Vp4]] |
| - | [[Category: | + | [[Category: Vp8*]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:57:11 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:57, 3 May 2008
Crystal structure of the rotavirus strain DS-1 VP8* core
Overview
The most intensively studied rotavirus strains initially attach to cells when the "heads" of their protruding spikes bind cell surface sialic acid. Rotavirus strains that cause disease in humans do not bind this ligand. The structure of the sialic acid binding head (the VP8* core) from the simian rotavirus strain RRV has been reported, and neutralization epitopes have been mapped onto its surface. We report here a 1.6-A resolution crystal structure of the equivalent domain from the sialic acid-independent rotavirus strain DS-1, which causes gastroenteritis in humans. Although the RRV and DS-1 VP8* cores differ functionally, they share the same galectin-like fold. Differences between the RRV and DS-1 VP8* cores in the region that corresponds to the RRV sialic acid binding site make it unlikely that DS-1 VP8* binds an alternative carbohydrate ligand in this location. In the crystals, a surface cleft on each DS-1 VP8* core binds N-terminal residues from a neighboring molecule. This cleft may function as a ligand binding site during rotavirus replication. We also report an escape mutant analysis, which allows the mapping of heterotypic neutralizing epitopes recognized by human monoclonal antibodies onto the surface of the VP8* core. The distribution of escape mutations on the DS-1 VP8* core indicates that neutralizing antibodies that recognize VP8* of human rotavirus strains may bind a conformation of the spike that differs from those observed to date.
About this Structure
2AEN is a Single protein structure of sequence from Human rotavirus a. Full crystallographic information is available from OCA.
Reference
High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain., Monnier N, Higo-Moriguchi K, Sun ZY, Prasad BV, Taniguchi K, Dormitzer PR, J Virol. 2006 Feb;80(3):1513-23. PMID:16415027 Page seeded by OCA on Sat May 3 18:57:11 2008
