Int. J. Mol. Sci. 2014, 15(4), 6797-6814; doi:10.3390/ijms15046797
Article

Modeling and Docking Studies on Novel Mutants (K71L and T204V) of the ATPase Domain of Human Heat Shock 70 kDa Protein 1

Received: 25 January 2014; in revised form: 3 April 2014 / Accepted: 4 April 2014 / Published: 22 April 2014
(This article belongs to the collection Proteins and Protein-Ligand Interactions)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: The purpose of exploring protein interactions between human adenovirus and heat shock protein 70 is to exploit a potentially synergistic interaction to enhance anti-tumoral efficacy and decrease toxicity in cancer treatment. However, the protein interaction of Hsp70 with E1A32 kDa of human adenovirus serotype 5 remains to be elucidated. In this study, two residues of ATPase domain of human heat shock 70 kDa protein 1 (PDB: 1 HJO) were mutated. 3D mutant models (K71L and T204V) using PyMol software were then constructed. The structures were evaluated by PROCHECK, ProQ, ERRAT, Verify 3D and ProSA modules. All evidence suggests that all protein models are acceptable and of good quality. The E1A32 kDa motif was retrieved from UniProt (P03255), as well as subjected to docking interaction with NBD, K71L and T204V, using the Autodock 4.2 program. The best lowest binding energy value of −9.09 kcal/mol was selected for novel T204V. Moreover, the protein-ligand complex structures were validated by RMSD, RMSF, hydrogen bonds and salt bridge analysis. This revealed that the T204V-E1A32 kDa motif complex was the most stable among all three complex structures. This study provides information about the interaction between Hsp70 and the E1A32 kDa motif, which emphasizes future perspectives to design rational drugs and vaccines in cancer therapy.
Keywords: adenovirus; Hsp70; PROCHECK; ProQ; ERRAT; Verify 3D; ProSA; docking
PDF Full-text Download PDF Full-Text [1049 KB, uploaded 19 June 2014 05:37 CEST]

Export to BibTeX |
EndNote


MDPI and ACS Style

Elengoe, A.; Naser, M.A.; Hamdan, S. Modeling and Docking Studies on Novel Mutants (K71L and T204V) of the ATPase Domain of Human Heat Shock 70 kDa Protein 1. Int. J. Mol. Sci. 2014, 15, 6797-6814.

AMA Style

Elengoe A, Naser MA, Hamdan S. Modeling and Docking Studies on Novel Mutants (K71L and T204V) of the ATPase Domain of Human Heat Shock 70 kDa Protein 1. International Journal of Molecular Sciences. 2014; 15(4):6797-6814.

Chicago/Turabian Style

Elengoe, Asita; Naser, Mohammed A.; Hamdan, Salehhuddin. 2014. "Modeling and Docking Studies on Novel Mutants (K71L and T204V) of the ATPase Domain of Human Heat Shock 70 kDa Protein 1." Int. J. Mol. Sci. 15, no. 4: 6797-6814.

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert