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A Novel Protein Interaction between Nucleotide Binding Domain of Hsp70 and p53 Motif
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,...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451777/ https://www.ncbi.nlm.nih.gov/pubmed/26098630 http://dx.doi.org/10.1155/2015/391293 |
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author | Elengoe, Asita Naser, Mohammed Abu Hamdan, Salehhuddin |
author_facet | Elengoe, Asita Naser, Mohammed Abu Hamdan, Salehhuddin |
author_sort | Elengoe, Asita |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4451777 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-44517772015-06-18 A Novel Protein Interaction between Nucleotide Binding Domain of Hsp70 and p53 Motif Elengoe, Asita Naser, Mohammed Abu Hamdan, Salehhuddin Int J Genomics Research Article 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. Hindawi Publishing Corporation 2015 2015-05-18 /pmc/articles/PMC4451777/ /pubmed/26098630 http://dx.doi.org/10.1155/2015/391293 Text en Copyright © 2015 Asita Elengoe et al. https://creativecommons.org/licenses/by/3.0/ 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. |
spellingShingle | Research Article Elengoe, Asita Naser, Mohammed Abu Hamdan, Salehhuddin A Novel Protein Interaction between Nucleotide Binding Domain of Hsp70 and p53 Motif |
title | A Novel Protein Interaction between Nucleotide Binding Domain of Hsp70 and p53 Motif |
title_full | A Novel Protein Interaction between Nucleotide Binding Domain of Hsp70 and p53 Motif |
title_fullStr | A Novel Protein Interaction between Nucleotide Binding Domain of Hsp70 and p53 Motif |
title_full_unstemmed | A Novel Protein Interaction between Nucleotide Binding Domain of Hsp70 and p53 Motif |
title_short | A Novel Protein Interaction between Nucleotide Binding Domain of Hsp70 and p53 Motif |
title_sort | novel protein interaction between nucleotide binding domain of hsp70 and p53 motif |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451777/ https://www.ncbi.nlm.nih.gov/pubmed/26098630 http://dx.doi.org/10.1155/2015/391293 |
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