PMID: 9182733Jun 1, 1997Paper

Selective binding of N-acetylglucosamine to the chicken hepatic lectin

The Biochemical Journal
L BurrowsK Drickamer

Abstract

Among Ca2+-dependent (C-type) animal lectins, the chicken hepatic lectin (CHL) is unique in displaying almost complete selectivity for N-acetylglucosamine over other monosaccharide ligands. The crystal structures of the carbohydrate-recognition domain (CRD) from serum mannose-binding protein (MBP) and of a complex between the CRD from liver MBP and the methyl glycoside of N-acetylglucosamine were used to model the binding site in CHL. Substitution of portions of CHL into the MBP framework did not substantially increase selectivity. A bacterial expression system for the CRD of CHL was developed so that specific residues predicted to be near the 2-acetamido substituent of N-acetylglucosamine could be altered by site-directed mutagenesis. The results indicate that the ligand is bound to CHL in the same orientation as it binds to liver MBP. A tyrosine and a valine residue that probably contact the the N-acetyl group have been identified. These results, together with studies of ligand-binding selectivity, suggest that these residues form part of a binding pocket for the N-acetyl group, which confers selective binding of N-acetylglucosamine.

Citations

Aug 4, 2012·Molecular & Cellular Proteomics : MCP·Harald NothaftChristine M Szymanski
Oct 26, 2002·The Journal of Biological Chemistry·Lucy EastClare M Isacke
Dec 13, 2005·The FEBS Journal·Alex N Zelensky, Jill E Gready
Sep 2, 1999·Current Biology : CB·A LoukasR M Maizels

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