| Literature DB >> 23886951 |
Svetlana N Kovalchuk1, Irina V Chikalovets, Oleg V Chernikov, Valentina I Molchanova, Wei Li, Valery A Rasskazov, Pavel A Lukyanov.
Abstract
An amino acid sequence of GalNAc/Gal-specific lectin from the mussel Crenomytilus grayanus (CGL) was determined by cDNA sequencing. CGL consists of 150 amino acid residues, contains three tandem repeats with high sequence similarities to each other (up to 73%) and does not belong to any known lectins family. According to circular dichroism results CGL is a β/α-protein with the predominance of β-structure. CGL was predicted to adopt a ß-trefoil fold. The lectin exhibits antibacterial activity and might be involved in the recognition and clearance of bacterial pathogens in the shellfish.Entities:
Keywords: Amino acid sequence; Antibacterial activity; Crenomytilus grayanus; GalNAc/Gal-specific lectin; ß-trefoil fold
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Year: 2013 PMID: 23886951 DOI: 10.1016/j.fsi.2013.07.011
Source DB: PubMed Journal: Fish Shellfish Immunol ISSN: 1050-4648 Impact factor: 4.581