| Popis: |
Lectins are proteins of a non-immune nature with activity against microorganisms, insects, and tumor cells. The aim of this work was to predict the physicochemical characteristics, structure, and functional properties of a Bauhinia holophylla lectin (BhL), sequenced from genomic material obtained from calli cultures, through bioinformatics tools. The results showed a high similarity between the Bhl gene and nucleotide sequences that encode lectins expressed by Bauhinia species and a high identity between the protein sequence of BhL and lectins from B. forficata (90%), B. variegata (79.04%), B. purpurea (78.01%), and B. ungulata (85.27%). BhL has 289 amino acids, of which 30, 85, and 174 residues are related to α-helix, β-sheet, and disordered regions, respectively. Their estimated molecular weight is 31.9 kDa and the theoretical isoelectric point is 5.79. Bauhinia holophylla lectin possibly undergoes phosphorylation and glycosylation at specific sites. Conserved protein domains, catalytic sites, and conserved amino acids were observed in BhL, bringing it closer to lectin families from other legume species. The prediction signaled the presence of a sequence of 28 amino acids at the N-terminal end of BhL, with a high hydropathicity index and conceptualized as a signal peptide. The molecular function predicted for BhL was associated with carbohydrate recognition activity. BhL could be an extracellular protein, and its three-dimensional structure showed 78.82% identity with the B. purpurea lectin. |
