ArticleActa crystallographica. Section F, Structural biology communications2015
Structure of a lectin from the sea mussel Crenomytilus grayanus (CGL).
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Taxonomic Distribution and Molecular Evolution of Mytilectins.Marine drugs · 2023Review
- Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022Review
- Mutagenesis Studies and Structure-function Relationships for GalNAc/Gal-Specific Lectin from the Sea Mussel Crenomytilus grayanus.Marine drugs · 2018Article
- Computational design of a symmetrical β-trefoil lectin with cancer cell binding activity.Scientific reports · 2017Article
- Antiviral lectins: Selective inhibitors of viral entry.Antiviral research · 2017Review
- Crystal structure of MytiLec, a galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types.Scientific reports · 2016Article
- cDNA and Gene Structure of MytiLec-1, A Bacteriostatic R-Type Lectin from the Mediterranean Mussel (Mytilus galloprovincialis).Marine drugs · 2016Article
- Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
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.
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