|
|
| Line 1: |
Line 1: |
| [[Image:3by3.jpg|left|200px]] | | #REDIRECT [[3d26]] This PDB entry is obsolete and replaced by 3d26 |
| | |
| <!--
| |
| The line below this paragraph, containing "STRUCTURE_3by3", creates the "Structure Box" on the page.
| |
| You may change the PDB parameter (which sets the PDB file loaded into the applet)
| |
| or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| |
| or leave the SCENE parameter empty for the default display.
| |
| -->
| |
| {{STRUCTURE_3by3| PDB=3by3 | SCENE= }}
| |
| | |
| '''Norwalk P domain A-trisaccharide complex'''
| |
| | |
| | |
| ==Overview==
| |
| Noroviruses are positive sense, single-stranded RNA viruses that cause acute gastroenteritis. They recognize human histo-blood group antigens as receptors in a strain-specific manner. The structures presented here sought to elucidate the structural basis for differences in ligand recognition of noroviruses from different genogroups, the prototypic Norwalk virus (NV, GI-1) and VA387 (GII-4), which recognize the same A-antigen, but differ in the inability of NV to bind to the B-antigen. Two forms of the receptor-binding domain of the norovirus coat protein, the P domain and the P polypeptide, that were previously shown to differ in receptor binding and P particle formation properties were studied. Comparison of the structures of the NV P domain with and without A-trisaccharide and the NV P polypeptide reveal no major ligand-induced changes. The 2.3 A co-crystal structure reveals that the A-trisaccharide binds to the NV P domain through interactions with residues Ser377, Asp327, His329, and Ser380 in a mode distinct from that previously reported for the VA387 P domain-A trisaccharide complex. Mutational analyses confirm the importance of these residues in NV P particle binding to native A-antigen. The alpha-GalNac residue unique to the A-trisaccharide is buried deeply in the NV binding pocket, unlike in the structures of A- and B-trisaccharides bound to VA387 P domain where the alpha-fucose residue forms the most protein contacts. The A-trisaccharide binding mode seen in the NV P domain complex cannot be sterically accommodated in the VA387 P domain.
| |
| | |
| ==About this Structure==
| |
| 3BY3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BY3 OCA].
| |
| | |
| ==Reference==
| |
| Structural basis for the receptor binding specificity of the Norwalk virus., Bu W, Mamedova A, Tan M, Xia M, Jiang X, Hegde RS, J Virol. 2008 Apr 2;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18385236 18385236]
| |
| [[Category: Norwalk virus]]
| |
| [[Category: Single protein]]
| |
| [[Category: Bu, W.]]
| |
| [[Category: Hegde, R.]]
| |
| [[Category: Norwalk p domain a trisaccaride complex]]
| |
| [[Category: Viral protein]]
| |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:50:16 2008''
| |
This PDB entry is obsolete and replaced by 3d26
