In silico prediction, characterization, docking studies and molecular dynamics simulation of human p97 in complex with p37 cofactor.

ABSTRACT:

Background

The AAA + ATPase p97 is an essential unfoldase/segragase involved in a multitude of cellular processes. It functions as a molecular machine critical for protein homeostasis, homotypic membrane fusion events and organelle biogenesis during mitosis in which it acts in concert with cofactors p47 and p37. Cofactors assist p97 in extracting and unfolding protein substrates through ATP hydrolysis. In contrast to other p97's cofactors, p37 uniquely increases the ATPase activity of p97. Disease-causing mutations in p97, including mutations that cause neurodegenerative diseases, increase cofactor association with its N-domain, ATPase activity and improper substrate processing. Upregulation of p97 has also been observed in various cancers. This study aims towards the characterizat

SUBMITTER: Mirzadeh A 

PROVIDER: S-EPMC9464413 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature