Intrinsically disordered proteins: modes of binding with emphasis on disordered domains

TY - JOUR

T1 - Intrinsically disordered proteins

T2 - modes of binding with emphasis on disordered domains

AU - Morris, Owen Michael

AU - Torpey, James Hilary

AU - Isaacson, Rivka Leah

N1 - Funding Information: This work was supported by the Biotechnology and Biological Sciences Research Council (grant nos. BB/N006267/1; BB/S006877/1). Publisher Copyright: ©

PY - 2021/10/1

Y1 - 2021/10/1

N2 - Our notions of protein function have long been determined by the protein structure-function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly challenged. Interactions involving intrinsically disordered proteins (IDPs) have indicated a significant degree of disorder present in the bound state, ranging from static disorder to complete disorder, termed 'random fuzziness'. This review assesses the anatomy of an IDP and relates how its intrinsic properties permit promiscuity and allow for the various modes of interaction. Furthermore, a mechanistic overview of the types of disordered domains is detailed, while also relating to a recent example and the kinetic and thermodynamic principles governing its formation.

AB - Our notions of protein function have long been determined by the protein structure-function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly challenged. Interactions involving intrinsically disordered proteins (IDPs) have indicated a significant degree of disorder present in the bound state, ranging from static disorder to complete disorder, termed 'random fuzziness'. This review assesses the anatomy of an IDP and relates how its intrinsic properties permit promiscuity and allow for the various modes of interaction. Furthermore, a mechanistic overview of the types of disordered domains is detailed, while also relating to a recent example and the kinetic and thermodynamic principles governing its formation.

KW - fuzzy binding

KW - intrinsic disorder

KW - protein folding

UR - http://www.scopus.com/inward/record.url?scp=85117856008&partnerID=8YFLogxK

U2 - 10.1098/rsob.210222

DO - 10.1098/rsob.210222

M3 - Article

C2 - 34610267

AN - SCOPUS:85117856008

SN - 2046-2441

VL - 11

SP - 210222

JO - Open Biology

JF - Open Biology

IS - 10

M1 - 210222

ER -