3WV6

Crystal Structure of a protease-resistant mutant form of human galectin-9

3WV6 の概要

• エントリーDOI: 10.2210/pdb3wv6/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900004 PRD_900008
• 分子名称: Galectin-9, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: beta sandwich, carbohydrate-binding, oligosaccharide, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68337.94

構造登録者

Yoshida, H.,Kamitori, S. (登録日: 2014-05-16, 公開日: 2015-05-20, 最終更新日: 2023-11-08)

主引用文献

Yoshida, H.,Nishi, N.,Wada, K.,Nakamura, T.,Hirashima, M.,Kuwabara, N.,Kato, R.,Kamitori, S.
X-ray structure of a protease-resistant mutant form of human galectin-9 having two carbohydrate recognition domains with a metal-binding site
Biochem.Biophys.Res.Commun., 490:1287-1293, 2017

PubMed Abstract: Galectin-9 (G9) is a tandem-repeat type β-galactoside-specific animal lectin having N-terminal and C-terminal carbohydrate recognition domains (N-CRD and C-CRD, respectively) joined by a linker peptide that is involved in the immune system. G9 is divalent in glycan binding, and structural information about the spatial arrangement of the two CRDs is very important for elucidating its biological functions. As G9 is protease sensitive due to the long linker, the protease-resistant mutant form of G9 (G9Null) was developed by modification of the linker peptide, while retaining its biological functions. The X-ray structure of a mutant form of G9Null with the replacement of Arg221 by Ser (G9Null_R221S) having two CRDs was determined. The structure of G9Null_R221S was compact to associate the two CRDs in the back-to-back orientation with a large interface area, including hydrogen bonds and hydrophobic interactions. A metal ion was newly found in the galectin structure, possibly contributing to the stable structure of protein. The presented X-ray structure was thought to be one of the stable structures of G9, which likely occurs in solution. This was supported by structural comparisons with other tandem-repeated galectins and the analyses of protein thermostability by CD spectra measurements.

PubMed: 28687490
DOI: 10.1016/j.bbrc.2017.07.009

実験手法

X-RAY DIFFRACTION (1.95 Å)