3I8T

N-terminal CRD1 domain of mouse Galectin-4 in complex with lactose

3I8T の概要

• エントリーDOI: 10.2210/pdb3i8t/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900008
• 分子名称: Galectin-4, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: s-type lectin, carbohydrate binding, molecular recognition, lectin, sugar binding protein
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19441.92

構造登録者

Brynda, J.,Krejcirikova, V.,Rezacova, P. (登録日: 2009-07-10, 公開日: 2011-02-23, 最終更新日: 2023-09-06)

主引用文献

Krejcirikova, V.,Pachl, P.,Fabry, M.,Maly, P.,Rezacova, P.,Brynda, J.
Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition
Acta Crystallogr.,Sect.D, 67:204-211, 2011

PubMed Abstract: Galectin-4, a member of the tandem-repeat subfamily of galectins, participates in cell-membrane interactions and plays an important role in cell adhesion and modulation of immunity and malignity. The oligosaccharide specificity of the mouse galectin-4 carbohydrate-recognition domains (CRDs) has been reported previously. In this work, the structure and binding properties of the N-terminal domain CRD1 were further investigated and the crystal structure of CRD1 in complex with lactose was determined at 2.1 Å resolution. The lactose-binding affinity was characterized by fluorescence measurements and two lactose-binding sites were identified: a high-affinity site with a K(d) value in the micromolar range (K(d1) = 600 ± 70 µM) and a low-affinity site with K(d2) = 28 ± 10 mM.

PubMed: 21358051
DOI: 10.1107/S0907444911004082

実験手法

X-RAY DIFFRACTION (2.1 Å)