Intrinsically disordered N-terminal domain (NTD) of p53 interacts with mitochondrial PTP regulator Cyclophilin D
J. Zhao, X. Liu, A. Blayney, Y. Zhang, L. Gandy, F. Zhang, R. J. Linhardt, J. Chen, C. Baines, S. N. Loh, C. Wang
This study identifies the N-terminal domain (NTD) of p53 as the major binding site for Cyclophilin D, revealing dynamic electrostatic interactions and a minimal binding region for mPTP regulation.
Journal of Molecular Biology · May 1, 2022Peer-reviewedBiochemistry