Computational Characterisation, Homology Modelling and Structure-based Functional Annotation of Very Low-density Lipoprotein Receptor of Salmo trutta fario

The present study was designed to enlist the physiochemical and functional properties of very low-density lipoprotein receptor Salmo trutta fario (brown trout), provide information about its three-dimensional structure interaction with partner molecules using standard bioinformatic tools. VLDL is a large flexible protein molecular weight around 95.9 kDa, relatively unstable, hydrophobic primary transmembrane helix from N-786 C-808. All 70 Cysteine residues (except four) are in disulphide bonding state. Secondary analysis shows that most has predominant random coiled configuration followed by extended strands. Six Epidermal growth factor-like domains two EGF-like-Ca2+ binding were predicted. plays crucially important role various metabolic pathways including vitellogenesis fishes. Understanding structural will facilitate better understanding dynamics designing experimental procedures.