2kmb

From Proteopedia

Revision as of 15:30, 30 October 2007

COMPLEX OF 3'-NEUAC-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A

Overview

Rat serum mannose-binding protein in which residues 211-213 have been, changed to the Lys-Lys-Lys sequence found in E-selectin binds HL-60 cells, and the oligosaccharide 3'-NeuAc-Le(x). To understand how this mutant, designated K3, mimics the carbohydrate-binding properties of E-selectin, structures of K3 alone and in complexes with 3'-NeuAc-Le(x), 3'-sulfo-Le(x) and 4'-sulfo-Le(x) have been determined at 1.95-2.1 A, resolution by X-ray crystallography. The region of K3 that interacts with, bound oligosaccharides superimposes closely with the corresponding region, of unliganded E-selectin. In each of the oligosaccharide-protein, complexes, the 2- and 3-OH of Fuc coordinate Ca2+ and form a network of, cooperative hydrogen bonds with amino acid side chains that also, coordinate the Ca2+. ... [(full description)]

About this Structure

2KMB is a [Single protein] structure of sequence from [Rattus norvegicus] with CA and CL as [ligands]. Structure known Active Sites: 11, 12, 13, 21, 22, 23, 31, 32 and 33. Full crystallographic information is available from [OCA].

Reference

Structure of a selectin-like mutant of mannose-binding protein complexed with sialylated and sulfated Lewis(x) oligosaccharides., Ng KK, Weis WI, Biochemistry. 1997 Feb 4;36(5):979-88. PMID:9033386

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