Structural highlights
FunctionPublication Abstract from PubMedThe three-dimensional structure of Dioclea reflexa seed lectin (DrfL) was studied in detail by a combination of X-ray crystallography, molecular docking and molecular dynamics. DrfL was purified by affinity chromatography using Sephadex G-50 matrix. Its primary structure was obtained by mass spectrometry, and crystals belonging to orthorhombic space group P212121 were grown by the vapor diffusion method at 293K. The crystal structure was solved at 1.765A and was very similar to that of other lectins from the same subtribe. The structure presented Rfactor and Rfree of 21.69% and 24.89%, respectively, with no residues in nonallowed regions of Ramachandran plot. Similar to other Diocleinae lectins, DrfL was capable of relaxing aortic rings via NO induction, with CRD participation, albeit with low intensity (32%). In silico analysis results demonstrated that DrfL could strongly interact with complex N-glycans, components of blood vessel glycoconjugates. Despite the high similarity among Diocleinae lectins, it was also reported that each lectin has unique CRD properties that influence carbohydrate binding, resulting in different biological effects presented by these molecules. Structural studies of a vasorelaxant lectin from Dioclea reflexa Hook seeds: Crystal structure, molecular docking and dynamics.,Pinto-Junior VR, Osterne VJ, Santiago MQ, Correia JL, Pereira-Junior FN, Leal RB, Pereira MG, Chicas LS, Nagano CS, Rocha BA, Silva-Filho JC, Ferreira WP, Rocha CR, Nascimento KS, Assreuy AM, Cavada BS Int J Biol Macromol. 2017 Jan 24;98:12-23. doi: 10.1016/j.ijbiomac.2017.01.092. PMID:28130130[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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