The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor
| Autor: | Jennifer L. McKimm-Breschkin, Joseph N. Varghese, James B. Caldwell, Peter M. Colman, Alexander A. Kortt |
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| Rok vydání: | 1992 |
| Předmět: |
Arginine
Macromolecular Substances Protein Conformation Stereochemistry Orthomyxoviridae Neuraminidase Biochemistry chemistry.chemical_compound Residue (chemistry) X-Ray Diffraction Structural Biology Carboxylate Molecular Biology chemistry.chemical_classification Fourier Analysis biology Glycosidic bond biology.organism_classification N-Acetylneuraminic Acid Sialic acid chemistry Sialic Acids biology.protein Receptors Virus N-Acetylneuraminic acid |
| Zdroj: | Proteins: Structure, Function, and Genetics. 14:327-332 |
| ISSN: | 1097-0134 0887-3585 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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