摘要
Lycoris radiata mannose-binding lectin（LRL） is a protein which binds mannose residues specifically. The maturation peptide and three mannose-binding domains（residues 49-57, 80-88 and 113--121） of LRL were identified by sequence analysis. The 3D structure of LRL constructed by homology modeling shaped a flstular triangular prism. Three flanks of the prism are mainly composed of β-sheets and each flank has a mannose-binding domain. According to the docking and dynamics simulation, the bindings of residues 49--57 and 80--88 with mannose are more stable than that of residues 113--121 with it. The key residues for binding mannose are Gin80, Asp82, Ash84 and Tyr88. The study preliminarily analyzed the interaction sites and mechanism of LRL with mannoses, which could be useful for the study on insect-resistance and related drug discovery of LRL.
Lycoris radiata mannose-binding lectin（LRL） is a protein which binds mannose residues specifically. The maturation peptide and three mannose-binding domains（residues 49-57, 80-88 and 113--121） of LRL were identified by sequence analysis. The 3D structure of LRL constructed by homology modeling shaped a flstular triangular prism. Three flanks of the prism are mainly composed of β-sheets and each flank has a mannose-binding domain. According to the docking and dynamics simulation, the bindings of residues 49--57 and 80--88 with mannose are more stable than that of residues 113--121 with it. The key residues for binding mannose are Gin80, Asp82, Ash84 and Tyr88. The study preliminarily analyzed the interaction sites and mechanism of LRL with mannoses, which could be useful for the study on insect-resistance and related drug discovery of LRL.
基金
National Natural Science Foundation of China
