Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain

被引：51

作者：

Nagae, Masamichi ^{[1
]}

Nishi, Nozomu ^{[2
]}

Murata, Takeomi ^{[3
]}

Usui, Taichi ^{[3
]}

Nakamura, Takanori ^{[2
]}

Wakatsuki, Soichi ^{[1
]}

Kato, Ryuichi ^{[1
]}

机构：

[1] High Energy Accelerator Res Org, Inst Mat Struct Sci, Photon Factory, Struct Biol Res Ctr, Tsukuba, Ibaraki 3050801, Japan

[2] Kagawa Univ, Fac Med, Dept Endocrinol, Kagawa 7610793, Japan

[3] Shizuoka Univ, Fac Agr, Dept Appl Biol Chem, Shizuoka 4228529, Japan

来源：

GLYCOBIOLOGY | 2009年 / 19卷 / 02期

关键词：

CRYSTAL-STRUCTURE; BINDING; PROGRAM; FAMILY; SPECIFICITY; REVEALS; LECTINS;

D O I：

10.1093/glycob/cwn121

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Galectins are a family of beta-galactoside-specific lectins bearing a conserved carbohydrate recognition domain. Interactions between galectins and poly-N-acetyllactosamine sequences are critical in a variety of biological processes. Galectin-9, a member of the galectin family, has two carbohydrate recognition domains at both the N- and C-terminal regions. Here we report the crystal structure of the human galectin-9 N-terminal carbohydrate recognition domain in complex with N-acetyllactosamine dimers and trimers. These complex structures revealed that the galectin-9 N-terminal carbohydrate recognition domain can recognize internal N-acetyllactosamine units within poly-N-acetyllactosamine chains. Based on these complex structures, we propose two putative recognition modes for poly-N-acetyllactosamine binding by galectins.

引用

页码：112 / 117

页数：6

共 30 条

[1] Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes [J].