3VKN

Galectin-8 N-terminal domain in free form

3VKN の概要

• エントリーDOI: 10.2210/pdb3vkn/pdb
• 関連するPDBエントリー: 3VKL 3VKM 3VKO
• 分子名称: Galectin-8, CHLORIDE ION (3 entities in total)
• 機能のキーワード: bete-sandwich, carbohydrate binding, oligosaccharide, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (Probable): O00214
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34771.67

構造登録者

Kamitori, S.,Yoshida, H. (登録日: 2011-11-18, 公開日: 2012-09-12, 最終更新日: 2023-11-08)

主引用文献

Yoshida, H.,Yamashita, S.,Teraoka, M.,Itoh, A.,Nakakita, S.,Nishi, N.,Kamitori, S.
X-ray structure of a protease-resistant mutant form of human galectin-8 with two carbohydrate recognition domains
Febs J., 279:3937-3951, 2012

PubMed Abstract: Galectin-8 is a tandem-repeat-type β-galactoside-specific animal lectin possessing N-terminal and C-terminal carbohydrate recognition domains (N-CRD and C-CRD, respectively), with a difference in carbohydrate-binding specificity, involved in cell-matrix interaction, malignant transformation, and cell adhesion. N-CRD shows strong affinity for α2-3-sialylated oligosaccharides, a feature unique to galectin-8. C-CRD usually shows lower affinity for oligosaccharides but higher affinity for N-glycan-type branched oligosaccharides than does N-CRD. There have been many structural studies on galectins with a single carbohydrate recognition domain (CRD), but no X-ray structure of a galectin containing both CRDs has been reported. Here, the X-ray structure of a protease-resistant mutant form of human galectin-8 possessing both CRDs and the novel pseudodimer structure of galectin-8 N-CRD in complexes with α2-3-sialylated oligosaccharide ligands were determined. The results revealed a difference in specificity between N-CRD and C-CRD, and provided new insights into the association of CRDs and/or molecules of galectin-8.

PubMed: 22913484
DOI: 10.1111/j.1742-4658.2012.08753.x

実験手法

X-RAY DIFFRACTION (1.98 Å)