Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered.

ABSTRACT: There is increasing evidence that many intrinsically disordered regions (IDRs) in proteins play key functional roles through interactions with other proteins or nucleic acids. These interactions often exhibit a context-dependent structural behavior. We hypothesize that low complexity regions (LCRs), often found within IDRs, could have a role in inducing local structure in IDRs. To test this, we predicted IDRs in the human proteome and analyzed their structures or those of homologous sequences in the Protein Data Bank (PDB). We then identified two types of simple LCRs within IDRs: regions with only one (polyX or homorepeats) or with only two types of amino acids (polyXY). We were able to assign structural information from the PDB more often to these LCRs than to the surrounding IDRs (polyX

SUBMITTER: Goncalves-Kulik M 

PROVIDER: S-EPMC9405754 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature