| Literature DB >> 1438172 |
J N Varghese1, J L McKimm-Breschkin, J B Caldwell, A A Kortt, P M Colman.
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.Entities:
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Year: 1992 PMID: 1438172 DOI: 10.1002/prot.340140302
Source DB: PubMed Journal: Proteins ISSN: 0887-3585