1mwe
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(New page: 200px<br /><applet load="1mwe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mwe, resolution 1.7Å" /> '''THE X-RAY STRUCTURE O...)
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Revision as of 19:38, 20 November 2007
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THE X-RAY STRUCTURE OF A COMPLEX OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE COMPLEXED WITH SIALIC ACID AT 4 DEGREES C REVEALING A SECOND SIALIC ACID BINDING SITE
Overview
The x-ray structure of a complex of sialic acid (Neu5Ac) with, neuraminidase N9 subtype from A/tern/Australia/G70C/75 influenza virus at, 4 degrees C has revealed the location of a second Neu5Ac binding site on, the surface of the enzyme. At 18 degrees C, only the enzyme active site, contains bound Neu5Ac. Neu5Ac binds in the second site in the chair, conformation in a similar way to which it binds to hemagglutinin. The, residues that interact with Neu5Ac at this second site are mostly, conserved in avian strains, but not in human and swine strains, indicating, that it has some as-yet-unknown biological function in birds.
About this Structure
1MWE is a Single protein structure of sequence from Influenza a virus with NAG, SIA and CA as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.
Reference
Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases., Varghese JN, Colman PM, van Donkelaar A, Blick TJ, Sahasrabudhe A, McKimm-Breschkin JL, Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11808-12. PMID:9342319
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