2BAT

THE STRUCTURE OF THE COMPLEX BETWEEN INFLUENZA VIRUS NEURAMINIDASE AND SIALIC ACID, THE VIRAL RECEPTOR

Summary for 2BAT

• Entry DOI: 10.2210/pdb2bat/pdb
• Related: 1NN2
• Descriptor: NEURAMINIDASE N2, 2-acetamido-2-deoxy-4-O-sulfo-alpha-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: hydrolase(o-glycosyl)
• Biological source: Influenza A virus (A/Tokyo/3/1967(H2N2))
• Cellular location: Virion membrane (By similarity): P06820
• Total number of polymer chains: 1
• Total formula weight: 46386.03

Authors

Varghese, J.N.,Colman, P.M. (deposition date: 1992-08-10, release date: 1994-01-31, Last modification date: 2024-11-20)

Primary citation

Varghese, J.N.,McKimm-Breschkin, J.L.,Caldwell, J.B.,Kortt, A.A.,Colman, P.M.
The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor.
Proteins, 14:327-332, 1992

PubMed Abstract: Crystallographic studies of neuraminidase-sialic acid complexes indicate that sialic acid is distorted on binding the enzyme. Three arginine residues on the enzyme interact with the carboxylate group of the sugar which is observed to be equatorial to the saccharide ring as a consequence of its distorted geometry. The glycosidic oxygen is positioned within hydrogen-bonding distance of Asp-151, implicating this residue in catalysis.

PubMed: 1438172
DOI: 10.1002/prot.340140302

Experimental method

X-RAY DIFFRACTION (2 Å)