Structural, functional and phylogenetic characterization of basic fatty acid binding protein 10 (Fabp10) of Cyprinus carpio, in silico approach
Keywords:
structural and functional analysis, phylogenetic tree, physicochemical parameters, structure validation, molecular dockingAbstract
Fatty acid binding proteins (FABPs) belong to a multigene family of intracellular lipid binding proteins. The aim of the study was to identify the structure and properties of fatty acid binding protein
from the liver of Cyrpinus carpio. In silico analysis related to physicochemical properties, secondary
and tertiary structure predictions and functional analysis was performed by the use of bioinformatic
tools. A total of 8 protein sequences of fatty acid binding protein, representing different species of
Cypriniform fishes were retrieved using NCBI. They were stable, extracellular, with an average molecular weight ranging from 14 KDa to 16.13 KDa and alkaline in nature. The proteins were members
of the superfamily lipocalin. The secondary structure, predicted by SOPMA and PSIPRED indicate
that random coil and extended strands are the most predominant in the selected sequences. The best
tertiary structure model of the protein obtained by the use of the SWISS model was refined by Galaxy
Refine. SWISS model suggested the 2QO4 as one of the best homologous templates for the predicted
3D protein structure. No transmembrane structure was found and only one disordered region was
identified. The protein act as secretory. The present study is focused on in silico molecular docking of
FABP-10 and the ligand, cholic acid (CHO).
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