2D6O

Crystal structure of mouse galectin-9 N-terminal CRD in complex with N-acetyllactosamine dimer

2D6O の概要

• エントリーDOI: 10.2210/pdb2d6o/pdb
• 関連するPDBエントリー: 2D6K 2D6L 2D6M 2D6N 2D6P
• 分子名称: lectin, galactose binding, soluble 9, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: beta sandwich, carbohydrate binding protein, galectin, sugar binding protein, structural genomics
• 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: 19010.54

構造登録者

Nagae, M.,Nishi, N.,Nakamura, T.,Murata, T.,Wakatsuki, S.,Kato, R. (登録日: 2005-11-14, 公開日: 2006-09-26, 最終更新日: 2024-10-30)

主引用文献

Nagae, M.,Nishi, N.,Murata, T.,Usui, T.,Nakamura, T.,Wakatsuki, S.,Kato, R.
Crystal Structure of the Galectin-9 N-terminal Carbohydrate Recognition Domain from Mus musculus Reveals the Basic Mechanism of Carbohydrate Recognition
J.Biol.Chem., 281:35884-35893, 2006

PubMed Abstract: The galectins are a family of beta-galactoside-binding animal lectins with a conserved carbohydrate recognition domain (CRD). They have a high affinity for small beta-galactosides, but binding specificity for complex glycoconjugates varies considerably within the family. The ligand recognition is essential for their proper function, and the structures of several galectins have suggested their mechanism of carbohydrate binding. Galectin-9 has two tandem CRDs with a short linker, and we report the crystal structures of mouse galectin-9 N-terminal CRD (NCRD) in the absence and the presence of four ligand complexes. All structures form the same dimer, which is quite different from the canonical 2-fold symmetric dimer seen for galectin-1 and -2. The beta-galactoside recognition mechanism in the galectin-9 NCRD is highly conserved among other galectins. In the apo form structure, water molecules mimic the ligand hydrogen-bond network. The galectin-9 NCRD can bind both N-acetyllactosamine (Galbeta1-4GlcNAc) and T-antigen (Galbeta1-3GalNAc) with the proper location of Arg-64. Moreover, the structure of the N-acetyllactosamine dimer (Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAc) complex shows a unique binding mode of galectin-9. Finally, surface plasmon resonance assay showed that the galectin-9 NCRD forms a homophilic dimer not only in the crystal but also in solution.

PubMed: 16990264
DOI: 10.1074/jbc.M606648200

実験手法

X-RAY DIFFRACTION (1.78 Å)