Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.

ABSTRACT: Understanding signaling and other complex biological processes requires elucidating the critical roles of intrinsically disordered proteins (IDPs) and regions (IDRs), which represent ∼30% of the proteome and enable unique regulatory mechanisms. In this review, we describe the structural heterogeneity of disordered proteins that underpins these mechanisms and the latest progress in obtaining structural descriptions of conformational ensembles of disordered proteins that are needed for linking structure and dynamics to function. We describe the diverse interactions of IDPs that can have unusual characteristics such as "ultrasensitivity" and "regulated folding and unfolding". We also summarize the mounting data showing that large-scale assembly and protein phase separation occurs within a var

SUBMITTER: Csizmok V 

PROVIDER: S-EPMC5342629 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature