Universiti Teknologi Malaysia Institutional Repository

A novel protein interaction between nucleotide binding domain of Hsp70 and p53 motif

Elengoe, Asita and Naser, Mohammed Abu and Hamdan, Salehhuddin (2015) A novel protein interaction between nucleotide binding domain of Hsp70 and p53 motif. International Journal of Genomics, 2015 (391293). ISSN 2314-436X

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Official URL: http://dx.doi.org/10.1155/2015/391293

Abstract

Currently, protein interaction of Homo sapiens nucleotide binding domain (NBD) of heat shock 70 kDa protein (PDB: 1HJO) with p53 motif remains to be elucidated. The NBD-p53 motif complex enhances the p53 stabilization, thereby increasing the tumor suppression activity in cancer treatment. Therefore, we identified the interaction between NBD and p53 using STRING version 9.1 program. Then, we modeled the three-dimensional structure of p53 motif through homology modeling and determined the binding affinity and stability of NBD-p53 motif complex structure via molecular docking and dynamics (MD) simulation. Human DNA binding domain of p53 motif (SCMGGMNR) retrieved from UniProt (UniProtKB: P04637) was docked with the NBD protein, using the Autodock version 4.2 program. The binding energy and intermolecular energy for the NBD-p53 motif complex were -0.44 Kcal/mol and -9.90 Kcal/mol, respectively. Moreover, RMSD, RMSF, hydrogen bonds, salt bridge, and secondary structure analyses revealed that the NBD protein had a strong bond with p53 motif and the protein-ligand complex was stable. Thus, the current data would be highly encouraging for designing Hsp70 structure based drug in cancer therapy.

Item Type:Article
Uncontrolled Keywords:protein domain, protein interaction
Subjects:Q Science > QD Chemistry
Divisions:Biosciences and Medical Engineering
ID Code:55785
Deposited By: Practical Student
Deposited On:06 Oct 2016 04:00
Last Modified:15 Feb 2017 01:15

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