The importance of the compact disordered state in the fuzzy interactions between intrinsically disordered proteins
Dan Wang, Shaowen Wu, Dongdong Wang, Xingyu Song, Maohua Yang, Wolun Zhang, Shaohui Huang, Jingwei Weng, Zhijun Liu, Wenning Wang
Abstract
the compact disordered state of 4.1G-CTD is crucial for binding. Different from the short linear motifs (SLiMs) that are often found to mediate IDP interactions, 4.1G-CTD functions as an intrinsically disordered domain (IDD), which is a functional and structural unit similar to conventional protein domains. This work sheds light on the molecular recognition mechanism of IDPs/IDRs and expands the conventional structure-function paradigm in protein biochemistry.
Topics & Concepts
Intrinsically disordered proteinsState (computer science)Fuzzy logicComputer scienceMaterials sciencePhysicsArtificial intelligenceNuclear magnetic resonanceAlgorithmProtein Structure and DynamicsEnzyme Structure and FunctionHemoglobin structure and function