5duy

Publication Abstract from PubMed

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 A. The amino-acid sequence of CGL contains three homologous regions (73% similarity) and the folded protein has a beta-trefoil topology. Structural comparison of CGL with the closely related lectin MytiLec allowed description of the glycan-binding pockets.

Structure of a lectin from the sea mussel Crenomytilus grayanus (CGL).,Jakob M, Lubkowski J, O'Keefe BR, Wlodawer A Acta Crystallogr F Struct Biol Commun. 2015 Nov 1;71(Pt 11):1429-36. doi:, 10.1107/S2053230X15019858. Epub 2015 Oct 24. PMID:26527272^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.