3NV2

Crystal structure of human galectin-9 C-terminal CRD in complex with N-acetyllactosamine

3NV2 の概要

• エントリーDOI: 10.2210/pdb3nv2/pdb
• 関連するPDBエントリー: 3NV1 3NV3 3NV4
• 関連するBIRD辞書のPRD_ID: PRD_900019
• 分子名称: Galectin 9 short isoform variant, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, NICKEL (II) ION, ... (4 entities in total)
• 機能のキーワード: sugar binding, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16172.02

構造登録者

Yoshida, H.,Kamitori, S. (登録日: 2010-07-07, 公開日: 2010-09-22, 最終更新日: 2023-11-01)

主引用文献

Yoshida, H.,Teraoka, M.,Nishi, N.,Nakakita, S.,Nakamura, T.,Hirashima, M.,Kamitori, S.
X-ray structures of human galectin-9 C-terminal domain in complexes with a biantennary oligosaccharide and sialyllactose
J.Biol.Chem., 285:36969-36976, 2010

PubMed Abstract: Galectin-9, a tandem-repeat-type β-galactoside-specific animal lectin with two carbohydrate recognition domains (CRDs) at the N- and C-terminal ends, is involved in chemoattraction, apoptosis, and the regulation of cell differentiation and has anti-allergic effects. Its ability to recognize carbohydrates is essential for its biological functions. Human galectin-9 (hG9) has high affinity for branched N-glycan-type oligosaccharides (dissociation constants of 0.16-0.70 μM) and linear β1-3-linked poly-N-acetyllactosamines (0.09-8.3 μM) and significant affinity for the α2-3-sialylated oligosaccharides (17-34 μM). Further, its N-terminal CRD (hG9N) and C-terminal CRD (hG9C) differ in specificity. To elucidate this unique feature of hG9, x-ray structures of hG9C in the free form and in complexes with N-acetyllactosamine, the biantennary pyridylaminated oligosaccharide, and α2-3-sialyllactose were determined. They are the first x-ray structural analysis of C-terminal CRD of the tandem-repeat-type galectin. The results clearly revealed the mechanism by which branched and α2-3-sialylated oligosaccharides are recognized and explained the difference in specificity between hG9N and hG9C. Based on structural comparisons with other galectins, we propose that the wide entrance for ligand binding and the shallow binding site of hG9C are favorable for branched oligosaccharides and that Arg(221) is responsible for recognizing sialylated oligosaccharides.

PubMed: 20861009
DOI: 10.1074/jbc.M110.163402

実験手法

X-RAY DIFFRACTION (2.34 Å)