A molecular model for diacylglycerol acyltransferase from Mortierella ramanniana var. angulispora

Acyl CoA diacylglycerol acyltransferase (DGAT, EC 2.3.120) is recognized as a key player of cellular diacylglycerolmetabolism. It catalyzes the terminal, yet the committed step in triacylglycerol synthesis using diacylglycerol and fatty acyl CoAas substrates. The protein sequence of diacylglycerol acyltransferse (DGAT) Type 2B in Moretierella ramanniana var.angulispora (Protein_ID = {"type":"entrez-protein","attrs":{"text":"AAK84180.1","term_id":"15099961"}}AAK84180.1) was retrieved from GenBank. However, a structure is not yet available for thissequence. The 3D structure of DGAT Type 2B was modeled using a template structure (PDB ID: 1K30) obtained from Proteindatabank (PDB) identified by searching with position specific iterative BLAST (PSI-BLAST). The template (PDB ID: 1K30)describes the structure of DGAT from Cucurbita moschata. Modeling was performed using Modeller 9v2 and protein model ishence generated. The DGAT type 2B protein model was subsequently docked with six inhibitors (sphingosine; trifluoroperazine;phosphatidic acid; lysophospatidylserine; KCl; 1, 2-diolein) using AutoDock (a molecular docking program). The binding ofinhibitors to the protein model of DGAT type 2B is discussed.