5DUY

Structure of lectin from the sea mussel Crenomytilus grayanus

5DUY の概要

• エントリーDOI: 10.2210/pdb5duy/pdb
• 分子名称: GalNAc/Gal-specific lectin, GLYCEROL (3 entities in total)
• 機能のキーワード: lectin, sea vertebrate, recombinant, trefoil, sugar binding protein
• 由来する生物種: Crenomytilus grayanus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 125823.99

構造登録者

Lubkowski, J.,Jakob, M.,O'Keefe, B.,Wlodawer, A. (登録日: 2015-09-21, 公開日: 2015-11-11, 最終更新日: 2024-03-06)

主引用文献

Jakob, M.,Lubkowski, J.,O'Keefe, B.R.,Wlodawer, A.
Structure of a lectin from the sea mussel Crenomytilus grayanus (CGL).
Acta Crystallogr.,Sect.F, 71:1429-1436, 2015

PubMed Abstract: CGL is a 150 amino-acid residue lectin that was originally isolated from the sea mussel Crenomytilus grayanus. It is specific for binding GalNAc/Gal-containing carbohydrate moieties and in general does not share sequence homology with other known galectins or lectins. Since CGL displays antibacterial, antifungal and antiviral activities, and interacts with high affinity with mucin-type receptors, which are abundant on some cancer cells, knowledge of its structure is of significant interest. Conditions have been established for the expression, purification and crystallization of a recombinant variant of CGL. The crystal structure of recombinant CGL was determined and refined at a resolution of 2.12 Å. The amino-acid sequence of CGL contains three homologous regions (73% similarity) and the folded protein has a β-trefoil topology. Structural comparison of CGL with the closely related lectin MytiLec allowed description of the glycan-binding pockets.

PubMed: 26527272
DOI: 10.1107/S2053230X15019858

実験手法

X-RAY DIFFRACTION (2.12 Å)