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Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel

The c subunits, which constitute the c‐ring apparatus of the F(1)F(O)‐ATPase, could be the main components of the mitochondrial permeability transition pore (mPTP). The well‐known modulator of the mPTP formation and opening is the cyclophilin D (CyPD), a peptidyl‐prolyl cis‐trans isomerase. On the l...

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Autor principal: Nesci, Salvatore
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9790210/
https://www.ncbi.nlm.nih.gov/pubmed/35532281
http://dx.doi.org/10.1002/prot.26383
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author Nesci, Salvatore
author_facet Nesci, Salvatore
author_sort Nesci, Salvatore
collection PubMed
description The c subunits, which constitute the c‐ring apparatus of the F(1)F(O)‐ATPase, could be the main components of the mitochondrial permeability transition pore (mPTP). The well‐known modulator of the mPTP formation and opening is the cyclophilin D (CyPD), a peptidyl‐prolyl cis‐trans isomerase. On the loop, which connects the two hairpin α‐helix of c subunit, is present the unique proline residue (Pro (40)) that could be a biological target of CyPD. Indeed, the proline cis‐trans isomerization might provide the switch that interconverts the open/closed states of the pore by pulling out the c‐ring lipid plug.
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spelling pubmed-97902102022-12-28 Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel Nesci, Salvatore Proteins Perspective The c subunits, which constitute the c‐ring apparatus of the F(1)F(O)‐ATPase, could be the main components of the mitochondrial permeability transition pore (mPTP). The well‐known modulator of the mPTP formation and opening is the cyclophilin D (CyPD), a peptidyl‐prolyl cis‐trans isomerase. On the loop, which connects the two hairpin α‐helix of c subunit, is present the unique proline residue (Pro (40)) that could be a biological target of CyPD. Indeed, the proline cis‐trans isomerization might provide the switch that interconverts the open/closed states of the pore by pulling out the c‐ring lipid plug. John Wiley & Sons, Inc. 2022-05-19 2022-11 /pmc/articles/PMC9790210/ /pubmed/35532281 http://dx.doi.org/10.1002/prot.26383 Text en © 2022 The Author. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Perspective
Nesci, Salvatore
Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel
title Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel
title_full Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel
title_fullStr Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel
title_full_unstemmed Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel
title_short Protein folding and unfolding: proline cis‐trans isomerization at the c subunits of F(1)F(O)‐ATPase might open a high conductance ion channel
title_sort protein folding and unfolding: proline cis‐trans isomerization at the c subunits of f(1)f(o)‐atpase might open a high conductance ion channel
topic Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9790210/
https://www.ncbi.nlm.nih.gov/pubmed/35532281
http://dx.doi.org/10.1002/prot.26383
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