Каталог "Статии" | Списание

Structural, functional and phylogenetic characterization of basic fatty acid binding protein 10 (Fabp10) of Cyprinus carpio, in silico approach

Anila Hoda; Valbona Kolaneci

Б 1098

Източник - периодично издание: ЖИВОТНОВЪДНИ науки
Източник: Животновъдни науки
Година на издаване: 2022
Пор.№: 4
Страници: с. 41-58
Том: 59
Ключови думи: molecular docking, phylogenetic tree, physicochemical parameters, structural and functional analysis, structure validation

ISSN: 0514-7441
Анотация: 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).
Системен №: 133156
Website: https://animalscience-bg.org/page/en/details.php?article_id=769&tab=en