2obr
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2obr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obr OCA], [http://www.ebi.ac.uk/pdbsum/2obr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2obr RCSB]</span> | ||
}} | }} | ||
| Line 16: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2OBR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 2OBR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Norovirus Norovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OBR OCA]. |
==Reference== | ==Reference== | ||
Structural basis for the recognition of blood group trisaccharides by norovirus., Cao S, Lou Z, Tan M, Chen Y, Liu Y, Zhang Z, Zhang XC, Jiang X, Li X, Rao Z, J Virol. 2007 Jun;81(11):5949-57. Epub 2007 Mar 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17392366 17392366] | Structural basis for the recognition of blood group trisaccharides by norovirus., Cao S, Lou Z, Tan M, Chen Y, Liu Y, Zhang Z, Zhang XC, Jiang X, Li X, Rao Z, J Virol. 2007 Jun;81(11):5949-57. Epub 2007 Mar 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17392366 17392366] | ||
| - | [[Category: | + | [[Category: Norovirus]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cao, S.]] | [[Category: Cao, S.]] | ||
| Line 32: | Line 35: | ||
[[Category: p domain]] | [[Category: p domain]] | ||
| - | ''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 04:15:35 2008'' |
Revision as of 01:15, 31 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structures of P Domain of Norovirus VA387
Overview
Noroviruses are one of the major causes of nonbacterial gastroenteritis epidemics in humans. Recent studies on norovirus receptors show that different noroviruses recognize different human histo-blood group antigens (HBGAs), and eight receptor binding patterns of noroviruses have been identified. The P domain of the norovirus capsids is directly involved in this recognition. To determine the precise locations and receptor binding modes of HBGA carbohydrates on the viral capsids, a recombinant P protein of a GII-4 strain norovirus, VA387, was cocrystallized with synthetic type A or B trisaccharides. Based on complex crystal structures observed at a 2.0-A resolution, we demonstrated that the receptor binding site lies at the outermost end of the P domain and forms an extensive hydrogen-bonding network with the saccharide ligand. The A and B trisaccharides display similar binding modes, and the common fucose ring plays a key role in this interaction. The extensive interface between the two protomers in a P dimer also plays a crucial role in the formation of the receptor binding interface.
About this Structure
2OBR is a Single protein structure of sequence from Norovirus. Full crystallographic information is available from OCA.
Reference
Structural basis for the recognition of blood group trisaccharides by norovirus., Cao S, Lou Z, Tan M, Chen Y, Liu Y, Zhang Z, Zhang XC, Jiang X, Li X, Rao Z, J Virol. 2007 Jun;81(11):5949-57. Epub 2007 Mar 28. PMID:17392366
Page seeded by OCA on Mon Mar 31 04:15:35 2008
Categories: Norovirus | Single protein | Cao, S. | Jiang, X. | Li, X. | Lou, Z. | Rao, Z. | Zhang, X C. | Crystal structure | Norovirus va387 | P domain
