3d26: Difference between revisions

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~~'''Unreleased structure'''~~

[[Image:3d26.jpg|left|200px]]

The ~~entry~~ 3d26 ~~is ON HOLD~~

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~~Authors: Hegde, R., Bu, W.~~

'''Norwalk P domain A-trisaccharide complex'''

~~Description: 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.

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==About this Structure==

3D26 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3by3 3by3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D26 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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:3d26.jpg|left|200px]]
-The entry 3d26 is ON HOLD
+<!--
+The line below this paragraph, containing "STRUCTURE_3d26", 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_3d26|  PDB=3d26  |  SCENE=  }}
-Authors: Hegde, R., Bu, W.
+'''Norwalk P domain A-trisaccharide complex'''
-Description: 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.
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 09:36:19 2008''
+==About this Structure==
+D26 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3by3 3by3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D26 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 Wed Jun 11 10:50:56 2008''