2b8h
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(New page: 200px<br /> <applet load="2b8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b8h, resolution 2.20Å" /> '''A/NWS/whale/Maine/1...)
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Revision as of 07:40, 18 November 2007
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A/NWS/whale/Maine/1/84 (H1N9) reassortant influenza virus neuraminidase
Overview
The X-ray structure of influenza virus neuraminidase (NA) isolated from, whale, subtype N9, has been determined at 2.2 A resolution and contains a, tetrameric protein in the asymmetric unit. In structures of NA determined, previously, a calcium ion is observed to coordinate amino acids near the, substrate-binding site. In three of the NA monomers determined here this, calcium is absent, resulting in structural alterations near the, substrate-binding site. These changes affect the conformation of residues, that participate in several key interactions between the enzyme and, substrate and provide at a molecular level the basis of the structural and, functional role of calcium in substrate and inhibitor binding. Several, sulfate ions were identified in complex with the protein. These are, located in the active site, occupying the space reserved for the substrate, (sialic acid) carboxylate, and in positions leading away from the, substrate-binding site. These sites offer a new opportunity for the design, of inhibitors of influenza virus NA.
About this Structure
2B8H is a Single protein structure of sequence from Influenza a virus with NAG, SO4, CL and GOL as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Full crystallographic information is available from OCA.
Reference
Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding., Smith BJ, Huyton T, Joosten RP, McKimm-Breschkin JL, Zhang JG, Luo CS, Lou MZ, Labrou NE, Garrett TP, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):947-52. Epub 2006, Aug 19. PMID:16929094
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