RT Journal Article
T1 The isolated armadillo-repeat domain of Plakophilin 1 is a monomer in solution with a low conformational stability.
A1 Giudici, A Marcela
A1 Hernandez-Cifre, Jose G
A1 Camara-Artigas, Ana
A1 Hornos, Felipe
A1 Martinez-Rodriguez, Sergio
A1 Carlos Alvarez-Perez, Juan
A1 Diaz-Cano, Ines
A1 Esther Farez-Vidal, Maria
A1 Neira, Jose L
K1 Analytical ultracentrifugation
K1 Circular dichroism
K1 Conformational stability
K1 Differential scanning calorimetry
K1 Fluorescence
K1 Scattering
AB Plakophilin 1 (PKP1) is a member of the armadillo repeat family of proteins. It serves as a scaffold component of desmosomes, which are key structural components for cell-cell adhesion. We have embarked on the biophysical and conformational characterization of the ARM domain of PKP1 (ARM-PKP1) in solution by using several spectroscopic (namely, fluorescence and circular dichroism (CD)) and biophysical techniques (namely, analytical ultracentrifugation (AUC), dynamic light scattering (DLS) and differential scanning calorimetry (DSC)). ARM-PKP1 was a monomer in solution at physiological pH, with a low conformational stability, as concluded from DSC experiments and thermal denaturations followed by fluorescence and CD. The presence or absence of disulphide bridges did not affect its low stability. The protein unfolded through an intermediate which has lost native-like secondary structure. ARM-PKP1 acquired a native-like structure in a narrow pH range (between pH 6.0 and 8.0), indicating that its adherent properties might only work in a very narrow pH range.
PB Elsevier Inc.
YR 2020
FD 2020-06-30
LK http://hdl.handle.net/10668/15918
UL http://hdl.handle.net/10668/15918
LA en
NO Giudici AM, Hernández-Cifre JG, Cámara-Artigas A, Hornos F, Martínez-Rodríguez S, Carlos Alvarez-Pérez J, et al. The isolated armadillo-repeat domain of Plakophilin 1 is a monomer in solution with a low conformational stability. J Struct Biol. 2020 Sep 1;211(3):107569.
DS RISalud
RD Apr 17, 2025