Disorder in a two-domain neuronal Ca²⁺-binding protein regulates domain stability and dynamics using ligand mimicry.

ABSTRACT: Understanding the interplay between sequence, structure and function of proteins has been complicated in recent years by the discovery of intrinsically disordered proteins (IDPs), which perform biological functions in the absence of a well-defined three-dimensional fold. Disordered protein sequences account for roughly 30% of the human proteome and in many proteins, disordered and ordered domains coexist. However, few studies have assessed how either feature affects the properties of the other. In this study, we examine the role of a disordered tail in the overall properties of the two-domain, calcium-sensing protein neuronal calcium sensor 1 (NCS-1). We show that loss of just six of the 190 residues at the flexible C-terminus is sufficient to severely affect stability, dynamics, and foldi

SUBMITTER: Staby L 

PROVIDER: S-EPMC7966663 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature