Moraes Filho RM, Rossiter JG, Cavalcanti Junior EA and Martins LSS
Legume lectins are a large group of proteins with similar structures, considerable amino acid sequence homology, and a variety of carbohydrate-binding specificities. Over 363 structures of plant lectins have been characterized, and they are the most extensively studied proteins of this class. In this study, in silico analyses were performed on legume lectin DNA and protein sequences of 35 species, aiming to find their conserved domains and to predict and compare their different tertiary structures, functions and molecular interactions. The protein sequences were aligned with ClustalW algorithm implemented in MEGA 6.06 software and a phylogenetic tree was constructed using the Neighborjoining method. Functional domain analysis revealed eight functional domains present in the four selected sequences representative of the main phylogenetic groups. The identified domains are related to carbohydrate binding, cytokinin binding and protein serine/threonine kinase activities. A model of tertiary structure of Vigna unguiculata was generated by Phyre2 server with the multitemplate feature, and its quality was verified by Molprobity and ProSA-web servers. Results of the molecular docking analysis revealed interaction sites with monosaccharides and a cytokinin from two different binding pockets. These results may provide theoretical informations into the molecular basis of legume lectin functions and structure.
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