Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid.
摘要：
The structure of the complex of NA with DANA, a transition state analog, has enabled us to identify and characterize the site of enzyme catalysis. The center of mass of bound inhibitor is 32 from the 4-fold axis of the tetramer, lodged at the end of a shallow crater of diameter 16 with a depth of 8 to 10 . There are 12 amino acid residues that directly bind DANA, with a further six conserved amino acids lining the active site pocket. The neuraminidase inhibitor complex provides a three-dimensional model which will be used to further the understanding of enzymatic hydrolysis and aid the design of specific, anti-neuraminidase antiviral compounds.
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关键词：
Influenza A virus Influenza B virus Sialic Acids X-Ray Diffraction Molecular Conformation Protein Conformation Binding Sites Mercury Neuraminidase N-Acetylneuraminic Acid
DOI：
10.1006/jmbi.1993.1461
被引量：
年份：
1993
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