Abstract:
:The 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 1.765Å 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.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
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 BSdoi
10.1016/j.ijbiomac.2017.01.092subject
Has Abstractpub_date
2017-05-01 00:00:00pages
12-23eissn
0141-8130issn
1879-0003pii
S0141-8130(16)32779-9journal_volume
98pub_type
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