In silico characterization and molecular modeling of MYB73 protein from Triticum aestivum L.

Abstract

Transcription factors (TFs) play vital regulatory roles in response to various abiotic stresses by interacting with cis-elements of several stress responsive genes. Functional properties of proteins are based on different intrinsic physicochemical characteristics. Protein engineering aiming to improve/modify kinetic properties or function of a protein is based on the knowledge of its physicochemical properties. Therefore, analysis of the structural features through different in silico tools is necessary to understand the properties of a protein at molecular level. In the present study, the MYB73 protein sequence revealed 94% homology with Myb4- like protein from Aegilopstauschii subsp. tauschii(Accession No. XP_020169006.1). The MYB proteins from various species showed three different conserved motifs. Alignment of the amino acid sequences using ClustalW revealed the presence of various conserved motifs. Serine was found to be the most abundant amino acid for MYB73, accounting for about 14.2%, followed by alanine, glutamate and leucine, whereas tyrosine and cysteine were the least abundant. The secondary structure generated using PDBsum has predicted a total of 6 α helices. The homology based 3D model of MYB73 was generated using Homo sapiens MYB transforming protein (PDB id- 1h8a) as a template by SWISS-MODEL server. Results revealed the presence of 100.0% amino acid residues in the most favored region. Ligand binding sites on protein were identified using FTSite server.