Intrinsically Disordered N-terminal Domain (NTD) of p53 Interacts with Mitochondrial PTP Regulator Cyclophilin D.

Binding Sites Peptidyl-Prolyl Isomerase F / chemistry Intrinsically Disordered Proteins / chemistry Mitochondrial Permeability Transition Pore / chemistry Molecular Dynamics Simulation Protein Domains Tumor Suppressor Protein p53 / chemistry
MD simulation NMR cyclophilin D mitochondrial permeability transition pore p53

Journal

Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R

Informations de publication

Date de publication:
15 05 2022
Historique:
received: 30 07 2021
revised: 11 03 2022
accepted: 15 03 2022
pubmed: 29 3 2022
medline: 3 5 2022
entrez: 28 3 2022
Statut: ppublish

Résumé

Mitochondrial permeability transition pore (mPTP) plays crucial roles in cell death in a variety of diseases, including ischemia/reperfusion injury in heart attack and stroke, neurodegenerative conditions, and cancer. To date, cyclophilin D is the only confirmed component of mPTP. Under stress, p53 can translocate into mitochondria and interact with CypD, triggering necrosis and cell growth arrest. However, the molecular details of p53/CypD interaction are still poorly understood. Previously, several studies reported that p53 interacts with CypD through its DNA-binding domain (DBD). However, using surface plasmon resonance (SPR), we found that both NTD-DBD, NTD and NTD (1-70) bind to CypD at ∼μM K

Identifiants

DOI: 10.1016/j.jmb.2022.167552 PMID: 35341741
pubmed: 35341741
pii: S0022-2836(22)00126-7
doi: 10.1016/j.jmb.2022.167552
pii:
doi:

Substances chimiques

Peptidyl-Prolyl Isomerase F 0
Intrinsically Disordered Proteins 0
Mitochondrial Permeability Transition Pore 0
Tumor Suppressor Protein p53 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

167552

Informations de copyright

Copyright © 2022 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Jing Zhao (J)

Center for Biotechnology and Interdisciplinary Studies, Troy, NY 12180, United States; Present address: College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.

Xinyue Liu (X)

Center for Biotechnology and Interdisciplinary Studies, Troy, NY 12180, United States; Present address: Department of Cell Biology, Harvard Medical School.

Alan Blayney (A)

Department Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, United States.

Yumeng Zhang (Y)

Department of Chemistry, University of Massachusetts, Amherst, MA 01003, United States.

Lauren Gandy (L)

Center for Biotechnology and Interdisciplinary Studies, Troy, NY 12180, United States; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, United States. Electronic address: https://twitter.com/a_science_life.

Paige Olivia Mirsky (PO)

Department of Biology, Syracuse University, Syracuse NY 13244.

Nathan Smith (N)

Center for Biotechnology and Interdisciplinary Studies, Troy, NY 12180, United States; Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180, United States.

Fuming Zhang (F)

Center for Biotechnology and Interdisciplinary Studies, Troy, NY 12180, United States; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, United States.

Robert J Linhardt (RJ)

Center for Biotechnology and Interdisciplinary Studies, Troy, NY 12180, United States; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, United States.

Jianhan Chen (J)

Department of Chemistry, University of Massachusetts, Amherst, MA 01003, United States.

Christopher Baines (C)

Dalton Cardiovascular Research Center, University of Missouri, Columbia, MO 65211, USA.

Stewart N Loh (SN)

Department Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, United States.

Chunyu Wang (C)

Center for Biotechnology and Interdisciplinary Studies, Troy, NY 12180, United States; Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180, United States. Electronic address: wangc5@rpi.edu.

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Classifications MeSH

questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Sites de fixation › Intrinsically Disordered N-terminal Domain...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines intrinsèquement désordonnées › Intrinsically Disordered N-terminal Domain...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines mitochondriales › Protéines de transport de la membrane mitochondriale › Pore de transition de perméabilité mitochondriale › Intrinsically Disordered N-terminal Domain...
questionsmedicales.fr › Sciences de l'information › Méthodologies informatiques › Simulation numérique › Simulation de dynamique moléculaire › Intrinsically Disordered N-terminal Domain...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Intrinsically Disordered N-terminal Domain...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Phosphoprotéines › Protéine p53 suppresseur de tumeur › Intrinsically Disordered N-terminal Domain...