MD simulations on the structure of onco-proteins p53: Wild-type and radioresistant mutant systems

Kholmirzo T. Kholmurodov; Evgenii A. Krasavin; Viktor A. Krylov; Ermuhammad B. Dushanov; Vladimir V. Korenkov; Kenji Yasuoka; Tetsu Narumi; Yousuke Ohno; Makoto Taiji; Toshikazu Ebisuzaki

MD simulations on the structure of onco-proteins p53: Wild-type and radioresistant mutant systems

Kholmirzo T. Kholmurodov, Evgenii A. Krasavin, Viktor A. Krylov, Ermuhammad B. Dushanov, Vladimir V. Korenkov, Kenji Yasuoka, Tetsu Narumi, Yousuke Ohno, Makoto Taiji, Toshikazu Ebisuzaki

Department of Mechanical Engineering

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Based on molecular dynamics (MD) simulation, a comparative analysis has been performed of the p53 dimer - DNA interaction for the wildtype and mutant Arg273His (R273H) proteins. The aim of this paper is to study the molecular mechanism of the p53 onco-protein and DNA binding. A comparative analysis shows that the R273H mutation has a significant effect on the p53-DNA interaction removing their close contact. The obtainedMD simulation results illustrate in detail the molecular mechanism of the conformations of the key amino acids in the p53-DNA binding domain, which is important for the physiological functioning of the p53 protein and understanding the origin of cancer.

Original language	English
Title of host publication	Molecular Dynamics of Nanobiostructures
Publisher	Nova Science Publishers, Inc.
Pages	179-208
Number of pages	30
ISBN (Print)	9781613243206
Publication status	Published - 2013 Jan

Keywords

MD simulations
Onco-protein p53
P53r273h mutation

ASJC Scopus subject areas

Chemical Engineering(all)
Physics and Astronomy(all)
Chemistry(all)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Cite this

@inbook{82ec0953234f4a728ddf3e75bc80fc64,

title = "MD simulations on the structure of onco-proteins p53: Wild-type and radioresistant mutant systems",

abstract = "Based on molecular dynamics (MD) simulation, a comparative analysis has been performed of the p53 dimer - DNA interaction for the wildtype and mutant Arg273His (R273H) proteins. The aim of this paper is to study the molecular mechanism of the p53 onco-protein and DNA binding. A comparative analysis shows that the R273H mutation has a significant effect on the p53-DNA interaction removing their close contact. The obtainedMD simulation results illustrate in detail the molecular mechanism of the conformations of the key amino acids in the p53-DNA binding domain, which is important for the physiological functioning of the p53 protein and understanding the origin of cancer.",

keywords = "MD simulations, Onco-protein p53, P53r273h mutation",

author = "Kholmurodov, {Kholmirzo T.} and Krasavin, {Evgenii A.} and Krylov, {Viktor A.} and Dushanov, {Ermuhammad B.} and Korenkov, {Vladimir V.} and Kenji Yasuoka and Tetsu Narumi and Yousuke Ohno and Makoto Taiji and Toshikazu Ebisuzaki",

year = "2013",

month = jan,

language = "English",

isbn = "9781613243206",

pages = "179--208",

booktitle = "Molecular Dynamics of Nanobiostructures",

publisher = "Nova Science Publishers, Inc.",

}

TY - CHAP

T1 - MD simulations on the structure of onco-proteins p53

T2 - Wild-type and radioresistant mutant systems

AU - Kholmurodov, Kholmirzo T.

AU - Krasavin, Evgenii A.

AU - Krylov, Viktor A.

AU - Dushanov, Ermuhammad B.

AU - Korenkov, Vladimir V.

AU - Yasuoka, Kenji

AU - Narumi, Tetsu

AU - Ohno, Yousuke

AU - Taiji, Makoto

AU - Ebisuzaki, Toshikazu

PY - 2013/1

Y1 - 2013/1

N2 - Based on molecular dynamics (MD) simulation, a comparative analysis has been performed of the p53 dimer - DNA interaction for the wildtype and mutant Arg273His (R273H) proteins. The aim of this paper is to study the molecular mechanism of the p53 onco-protein and DNA binding. A comparative analysis shows that the R273H mutation has a significant effect on the p53-DNA interaction removing their close contact. The obtainedMD simulation results illustrate in detail the molecular mechanism of the conformations of the key amino acids in the p53-DNA binding domain, which is important for the physiological functioning of the p53 protein and understanding the origin of cancer.

AB - Based on molecular dynamics (MD) simulation, a comparative analysis has been performed of the p53 dimer - DNA interaction for the wildtype and mutant Arg273His (R273H) proteins. The aim of this paper is to study the molecular mechanism of the p53 onco-protein and DNA binding. A comparative analysis shows that the R273H mutation has a significant effect on the p53-DNA interaction removing their close contact. The obtainedMD simulation results illustrate in detail the molecular mechanism of the conformations of the key amino acids in the p53-DNA binding domain, which is important for the physiological functioning of the p53 protein and understanding the origin of cancer.

KW - MD simulations

KW - Onco-protein p53

KW - P53r273h mutation

UR - http://www.scopus.com/inward/record.url?scp=84896150940&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84896150940&partnerID=8YFLogxK

M3 - Chapter

AN - SCOPUS:84896150940

SN - 9781613243206

SP - 179

EP - 208

BT - Molecular Dynamics of Nanobiostructures

PB - Nova Science Publishers, Inc.

ER -

MD simulations on the structure of onco-proteins p53: Wild-type and radioresistant mutant systems

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

Other files and links

Fingerprint

Cite this