5DUY
Structure of lectin from the sea mussel Crenomytilus grayanus
Summary for 5DUY
| Entry DOI | 10.2210/pdb5duy/pdb |
| Descriptor | GalNAc/Gal-specific lectin, GLYCEROL (3 entities in total) |
| Functional Keywords | lectin, sea vertebrate, recombinant, trefoil, sugar binding protein |
| Biological source | Crenomytilus grayanus |
| Total number of polymer chains | 6 |
| Total formula weight | 125823.99 |
| Authors | Lubkowski, J.,Jakob, M.,O'Keefe, B.,Wlodawer, A. (deposition date: 2015-09-21, release date: 2015-11-11, Last modification date: 2024-03-06) |
| Primary citation | 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 Cited by 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: 26527272DOI: 10.1107/S2053230X15019858 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.12 Å) |
Structure validation
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