2QWB
THE X-RAY STRUCTURE OF A COMPLEX OF SIALIC ACID AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
Summary for 2QWB
Entry DOI | 10.2210/pdb2qwb/pdb |
Descriptor | NEURAMINIDASE, alpha-D-mannopyranose-(1-2)-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, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
Functional Keywords | neuraminidase, influenza protein, drug resistant variant, sialic acid, second binding site, glycosylated protein, hydrolase |
Biological source | Influenza A virus |
Cellular location | Virion membrane (By similarity): P03472 |
Total number of polymer chains | 1 |
Total formula weight | 46275.16 |
Authors | Varghese, J.N. (deposition date: 1998-04-07, release date: 1998-11-11, Last modification date: 2024-04-03) |
Primary citation | Varghese, J.N.,Smith, P.W.,Sollis, S.L.,Blick, T.J.,Sahasrabudhe, A.,McKimm-Breschkin, J.L.,Colman, P.M. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure, 6:735-746, 1998 Cited by PubMed Abstract: Inhibitors of the influenza virus neuraminidase have been shown to be effective antiviral agents in humans. Several studies have reported the selection of novel influenza strains when the virus is cultured with neuraminidase inhibitors in vitro. These resistant viruses have mutations either in the neuraminidase or in the viral haemagglutinin. Inhibitors in which the glycerol sidechain at position 6 of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (Neu5Ac2en) has been replaced by carboxamide-linked hydrophobic substituents have recently been reported and shown to select neuraminidase variants. This study seeks to clarify the structural and functional consequences of replacing the glycerol sidechain of the inhibitor with other chemical constituents. PubMed: 9655825DOI: 10.1016/S0969-2126(98)00075-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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