biostudies-literatureUnknown90(11)Nesci SThe c subunits, which constitute the c-ring apparatus of the F₁ 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 (Pro₄₀ ) 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.Proteins2001-2005https://www.ebi.ac.uk/biostudies/studies/S-EPMC9790210biostudies-literatureProtein folding and unfolding: proline cis-trans isomerization at the c subunits of F₁ F_O -ATPase might open a high conductance ion channel.PMC9790210Nesci SfalseProtein folding and unfolding: proline cis-trans isomerization at the c subunits of F₁ F_O -ATPase might open a high conductance ion channel.The c subunits, which constitute the c-ring apparatus of the F₁ 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 (Pro₄₀ ) 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.2022-01-01T00:00:00Z2022 Nov2025-04-04T21:00:54.201Z2025-04-04T21:00:54.201ZS-EPMC97902103553228110.1002/prot.26383