Ontology highlight
ABSTRACT:
SUBMITTER: Jakob M
PROVIDER: S-EPMC4631594 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
Jakób Michał M Lubkowski Jacek J O'Keefe Barry R BR Wlodawer Alexander A
Acta crystallographica. Section F, Structural biology communications 20151024 Pt 11
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. Cond ...[more]