Homology modeling of the DNA binding and dimerization partner domains of E2F1 transcription factor protein in homo sapiens

E2F1 is a sole member of E2F transcription factors family that embraces a unique ability to mediate two contradictory processes of cell proliferation and apoptosis via numerous pathways. The atomistic structure of E2F protein would provide insight into understanding of the protein-DNA interaction in order to regulate crucial biological pathways. However, the high resolution structure of E2F1 protein is not yet fully crystallized. Here, we report the homology model of E2F1 covering residues 126 to 301 which comprises the DNA binding and dimerization partner domains. Structural construction and refinement of the model was done using MODELLER 9v9. The incorporation of a segment consists of residues 192 to 200 that resulted from the I-Tasser modeling prediction server. The RMSD for the final model structure is less than 1 Å after being superimposed with the template structures, 1CF7.pdb and 2AZE.pdb. The Ramachandran plot also showed that only 1.2 % of amino acid residues are in the disfavoured region. Interestingly, the developed model is found to resemble to one of the I-Tasser top predicted models.