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| {{STRUCTURE_2obt| PDB=2obt | SCENE= }} | | {{STRUCTURE_2obt| PDB=2obt | SCENE= }} |
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| '''Crystal Structures of P Domain of Norovirus VA387 in Complex with Blood Group Trisaccharides type B'''
| | ===Crystal Structures of P Domain of Norovirus VA387 in Complex with Blood Group Trisaccharides type B=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17392366}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17392366 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17392366}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Norovirus va387]] | | [[Category: Norovirus va387]] |
| [[Category: P domain]] | | [[Category: P domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:34:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:35:36 2008'' |
