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
Keyword(s):
Α Helix
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The c subunits, which constitutes the c-ring apparatus of the F F -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 ) 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.
2013 ◽
Vol 304
(5)
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pp. H649-H659
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2019 ◽
Vol 294
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pp. 10807-10818
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2011 ◽
Vol 286
(46)
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pp. 40184-40192
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