1e9l
From Proteopedia
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THE CRYSTAL STRUCTURE OF NOVEL MAMMALIAN LECTIN YM1 SUGGESTS A SACCHARIDE BINDING SITE
Overview
Ym1, a secretory protein synthesized by activated murine peritoneal, macrophages, is a novel mammalian lectin with a binding specificity to, GlcN. Lectins are responsible for carbohydrate recognition and for, mediating cell-cell and cell-extracellular matrix interactions in, microbes, plants, and animals. Glycosaminoglycan heparin/heparan sulfate, binding ability was also detected in Ym1. We report here the, three-dimensional structure of Ym1 at 2.5-A resolution by x-ray, crystallography. The crystal structure of Ym1 consists of two globular, domains, a beta/alpha triose-phosphate isomerase barrel domain and a small, alpha + beta folding domain. A notable electron density of sugar is, detected in the Ym1 crystal structure. The saccharide is located inside, the triose-phosphate isomerase domain at the COOH terminal end of the, beta-strands. Both hydrophilic and hydrophobic interactions are noted in, the sugar-binding site in Ym1. Despite the fact that Ym1 is not a, chitinase, structurally, Ym1 shares significant homology with chitinase A, of Serratia marcescens. Ym1 and chitinase A have a similar carbohydrate, binding cleft. This study provides new structure information, which will, lead to better understanding of the biological significance of Ym1 and its, putative gene members.
About this Structure
1E9L is a Single protein structure of sequence from Mus musculus with GCS as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of a novel mammalian lectin, Ym1, suggests a saccharide binding site., Sun YJ, Chang NC, Hung SI, Chang AC, Chou CC, Hsiao CD, J Biol Chem. 2001 May 18;276(20):17507-14. Epub 2001 Feb 15. PMID:11278670
Page seeded by OCA on Tue Nov 20 13:50:40 2007
Categories: Mus musculus | Single protein | Hsiao, C.D. | Sun, Y.J. | GCS | Inducible | Inflammation | Lectin | Secretory
