Updated protein domain annotation of the PARP protein family sheds new light on biological function.

ABSTRACT: AlphaFold2 and related computational tools have greatly aided studies of structural biology through their ability to accurately predict protein structures. In the present work, we explored AF2 structural models of the 17 canonical members of the human PARP protein family and supplemented this analysis with new experiments and an overview of recent published data. PARP proteins are typically involved in the modification of proteins and nucleic acids through mono or poly(ADP-ribosyl)ation, but this function can be modulated by the presence of various auxiliary protein domains. Our analysis provides a comprehensive view of the structured domains and long intrinsically disordered regions within human PARPs, offering a revised basis for understanding the function of these proteins. Among other

SUBMITTER: Suskiewicz MJ 

PROVIDER: S-EPMC10450202 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature