5CBL

Crystal structure of the C-terminal domain of human galectin-4 with lactose

5CBL の概要

• エントリーDOI: 10.2210/pdb5cbl/pdb
• 関連するPDBエントリー: 4XZP
• 関連するBIRD辞書のPRD_ID: PRD_900004
• 分子名称: Galectin-4, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: galectins, beta-galactosides binding, sugar binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67228.04

構造登録者

Rustiguel, J.K.,Nonato, M.C. (登録日: 2015-07-01, 公開日: 2015-11-04, 最終更新日: 2024-12-25)

主引用文献

Rustiguel, J.K.,Kumagai, P.S.,Dias-Baruffi, M.,Costa-Filho, A.J.,Nonato, M.C.
Recombinant expression, purification and preliminary biophysical and structural studies of C-terminal carbohydrate recognition domain from human galectin-4.
Protein Expr.Purif., 118:39-48, 2015

PubMed Abstract: Galectin-4 (Gal4), a tandem-repeat type galectin, is expressed in healthy epithelium of the gastrointestinal tract. Altered levels of Gal4 expression are associated with different types of cancer, suggesting its usage as a diagnostic marker as well as target for drug development. The functional data available for this class of proteins suggest that the wide spectrum of cellular activities reported for Gal4 relies on distinct glycan specificity and structural characteristics of its two carbohydrate recognition domains. In the present work, two independent constructs for recombinant expression of the C-terminal domain of human galectin-4 (hGal4-CRD2) were developed. His6-tagged and untagged recombinant proteins were overexpressed in Escherichia coli, and purified by affinity chromatography followed by gel filtration. Correct folding and activity of hGal4-CRD2 were assessed by circular dichroism and fluorescence spectroscopies, respectively. Diffraction quality crystals were obtained by vapor-diffusion sitting drop setup and the crystal structure of CRD2 was solved by molecular replacement techniques at 1.78 Å resolution. Our work describes the development of important experimental tools that will allow further studies in order to correlate structure and binding properties of hGal4-CRD2 and human galectin-4 functional activities.

PubMed: 26432949
DOI: 10.1016/j.pep.2015.09.026

実験手法

X-RAY DIFFRACTION (1.781 Å)