1E9L

The crystal structure of novel mammalian lectin Ym1 suggests a saccharide binding site

1E9L の概要

• エントリーDOI: 10.2210/pdb1e9l/pdb
• 分子名称: YM1 SECRETORY PROTEIN, 2-amino-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: macrophage secretory protein, inflammation, lectin, inducible, secretory
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42544.69

構造登録者

Hsiao, C.D.,Sun, Y.J. (登録日: 2000-10-21, 公開日: 2001-03-01, 最終更新日: 2024-10-23)

主引用文献

Sun, Y.J.,Chang, N.C.,Hung, S.I.,Chang, A.C.,Chou, C.C.,Hsiao, C.D.
The Crystal Structure of a Novel Mammalian Lectin, Ym1, Suggests a Saccharide Binding Site
J.Biol.Chem., 276:17507-, 2001

PubMed Abstract: 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.

PubMed: 11278670
DOI: 10.1074/JBC.M010416200

実験手法

X-RAY DIFFRACTION (2.5 Å)