{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang D"],"funding":["Ministry of Science and Technology of the People's Republic of China","National Natural Science Foundation of China"],"pagination":["2363-2377"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8864705"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(8)"],"pubmed_abstract":["The intrinsically disordered C-terminal domain (CTD) of protein 4.1G is able to specifically bind a 26-residue intrinsically disordered region of NuMA, forming a dynamic fuzzy complex. As one of a few cases of extremely fuzzy interactions between two intrinsically disordered proteins/regions (IDPs/IDRs) without induced folding, the principle of the binding is unknown. Here, we combined experimental and computational methods to explore the detailed mechanism of the interaction between 4.1G-CTD and NuMA. MD simulations suggest that the kinetic hub states in the structure ensemble of 4.1G-CTD are favorable in the fuzzy complex. The feature of these hub states is that the binding 'hot spot' motifs βA and βB exhibit β strand propensities and are well packed to each other. The binding between 4."],"journal":["Chemical science"],"pubmed_title":["The importance of the compact disordered state in the fuzzy interactions between intrinsically disordered proteins."],"pmcid":["PMC8864705"],"funding_grant_id":["2016YFA0501702","21877017","22073018"],"pubmed_authors":["Zhang W","Huang S","Liu Z","Wang D","Yang M","Wu S","Weng J","Wang W","Song X"],"additional_accession":[]},"is_claimable":false,"name":"The importance of the compact disordered state in the fuzzy interactions between intrinsically disordered proteins.","description":"The intrinsically disordered C-terminal domain (CTD) of protein 4.1G is able to specifically bind a 26-residue intrinsically disordered region of NuMA, forming a dynamic fuzzy complex. As one of a few cases of extremely fuzzy interactions between two intrinsically disordered proteins/regions (IDPs/IDRs) without induced folding, the principle of the binding is unknown. Here, we combined experimental and computational methods to explore the detailed mechanism of the interaction between 4.1G-CTD and NuMA. MD simulations suggest that the kinetic hub states in the structure ensemble of 4.1G-CTD are favorable in the fuzzy complex. The feature of these hub states is that the binding 'hot spot' motifs βA and βB exhibit β strand propensities and are well packed to each other. The binding between 4.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2025-04-19T13:17:36.328Z","creation":"2025-04-19T13:17:36.328Z"},"accession":"S-EPMC8864705","cross_references":{"pubmed":["35310482"],"doi":["10.1039/d1sc06825c"]}}