The c subunits, which constitute the c-ring apparatus of the F1 FO -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.

Nesci S. (2022). Protein folding and unfolding: proline cis-trans isomerization at the c subunits of F1FO-ATPase might open a high conductance ion channel. PROTEINS, 90(11), 2001-2005 [10.1002/prot.26383].

Protein folding and unfolding: proline cis-trans isomerization at the c subunits of F1FO-ATPase might open a high conductance ion channel

Nesci S.
2022

Abstract

The c subunits, which constitute the c-ring apparatus of the F1 FO -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
Nesci S. (2022). Protein folding and unfolding: proline cis-trans isomerization at the c subunits of F1FO-ATPase might open a high conductance ion channel. PROTEINS, 90(11), 2001-2005 [10.1002/prot.26383].
Nesci S.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/895762
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