1vpn: Difference between revisions

Revision as of 01:11, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1vpn.png

Template:STRUCTURE 1vpn

UNASSEMBLED POLYOMAVIRUS VP1 PENTAMERUNASSEMBLED POLYOMAVIRUS VP1 PENTAMER

Template:ABSTRACT PUBMED 9305654

About this StructureAbout this Structure

1VPN is a Single protein structure of sequence from Murine polyomavirus. Full crystallographic information is available from OCA.

ReferenceReference

High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding., Stehle T, Harrison SC, EMBO J. 1997 Aug 15;16(16):5139-48. PMID:9305654

Page seeded by OCA on Mon Jul 28 01:10:47 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1vpn.gif|left|200px]]
+{{Seed}}
+[[Image:1vpn.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1vpn|  PDB=1vpn  |  SCENE=  }}
-'''UNASSEMBLED POLYOMAVIRUS VP1 PENTAMER'''
+===UNASSEMBLED POLYOMAVIRUS VP1 PENTAMER===
-==Overview==
+<!--
-The crystal structure of a recombinant polyomavirus VP1 pentamer (residues 32-320) in complex with a branched disialylated hexasaccharide receptor fragment has been determined at 1.9 A resolution. The result extends our understanding of oligosaccharide receptor recognition. It also suggests a mechanism for enhancing the fidelity of virus assembly. We have previously described the structure of the complete polyomavirus particle complexed with this receptor fragment at 3.65 A. The model presented here offers a much more refined view of the interactions that determine carbohydrate recognition and allows us to assign additional specific contacts, in particular those involving the (alpha2,6)-linked, branching sialic acid. The structure of the unliganded VP1 pentamer, determined independently, shows that the oligosaccharide fits into a preformed groove and induces no measurable structural rearrangements. A comparison with assembled VP1 in the virus capsid reveals a rearrangement of residues 32-45 at the base of the pentamer. This segment may help prevent the formation of incorrectly assembled particles by reducing the likelihood that the C-terminal arm will fold back into its pentamer of origin.
+The line below this paragraph, {{ABSTRACT_PUBMED_9305654}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9305654 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9305654}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Virus assembly]]
 [[Category: Virus coat protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:46:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:10:47 2008''