NDLI: Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases.

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Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Van Donkelaar, A. Blick, T. J. Sahasrabudhe, A. Mckimm-breschkin, J. L. Varghese, J. N. Colman, P. M.
Description	Author Affiliation: Varghese JN ( Biomolecular Research Institute, 343 Royal Parade, Parkville, 3052 Australia. jose.varghese@bioresi.com.au);
Abstract	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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Influenza A Virus Enzymology N-Acetylneuraminic Acid Metabolism Neuraminidase Chemistry Viral Proteins Binding Sites Computer Simulation Crystallography, X-Ray Models, Molecular Molecular Sequence Data Protein Conformation Sequence Homology, Amino Acid Surface Properties Comparative Study Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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