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




Modeling and Docking Studies on Novel Mutants K71L and T204V of the ATPase Domain of Human Heat Shock 70 kDa Protein 1 - Descarga este documento en PDF. Documentación en PDF para descargar gratis. Disponible también para leer online.

Faculty of Bioscience and Medical Engineering, Universiti Teknologi Malaysia, Skudai, Johor 81310, Malaysia



These authors contributed equally to this work.





*

Author to whom correspondence should be addressed.



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. View Full-Text

Keywords: adenovirus; Hsp70; PROCHECK; ProQ; ERRAT; Verify 3D; ProSA; docking adenovirus; Hsp70; PROCHECK; ProQ; ERRAT; Verify 3D; ProSA; docking





Autor: Asita Elengoe * , Mohammed Abu Naser † and Salehhuddin Hamdan †

Fuente: http://mdpi.com/



DESCARGAR PDF




Documentos relacionados