Protein folding and unfolding: proline cis-trans isomerization at the c subunits of F1 FO -ATPase might open a high conductance ion channel.
Proteins
; 90(11): 2001-2005, 2022 11.
Article
em En
| MEDLINE
| ID: mdl-35532281
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.
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Base de dados:
MEDLINE
Assunto principal:
Prolina
/
Poro de Transição de Permeabilidade Mitocondrial
Idioma:
En
Ano de publicação:
2022
Tipo de documento:
Article