Structural highlights
Publication Abstract from PubMedA glycosylated lectin (CTL) with specificity for mannose and glucose has been detected and purified from seeds of Centrolobium tomentosum, a legume plant from Dalbergieae tribe. It was isolated by mannose-sepharose affinity chromatography. The primary structure was determined by tandem mass spectrometry and consists of 245 amino acids, similar to other Dalbergieae lectins. CTL structures were solved from two crystal forms, a monoclinic and a tetragonal, diffracted at 2.25 and 1.9 A, respectively. The carbohydrate recognition domain (CRD), metal-binding site and glycosylation site were characterized, and the structural basis for mannose/glucose-binding was elucidated. The lectin adopts the canonical dimeric organization of legume lectins. CTL showed acute inflammatory effect in paw edema model. The protein was subjected to ligand screening (dimannosides and trimannoside) by molecular docking, and interactions were compared with similar lectins possessing the same ligand specificity. This is the first crystal structure of mannose/glucose native seed lectin with proinflammatory activity isolated from the Centrolobium genus. Structural analysis of Centrolobium tomentosum seed lectin with inflammatory activity.,Almeida AC, Osterne VJ, Santiago MQ, Pinto-Junior VR, Silva-Filho JC, Lossio CF, Nascimento FL, Almeida RP, Teixeira CS, Leal RB, Delatorre P, Rocha BA, Assreuy AM, Nascimento KS, Cavada BS Arch Biochem Biophys. 2016 Apr 15;596:73-83. doi: 10.1016/j.abb.2016.03.001. Epub, 2016 Mar 3. PMID:26946944[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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