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- W2085405404 abstract "Intrinsically disordered proteins play important roles in mediating regulatory interactions. While many of these proteins fold upon binding to targets, others appear to be only transiently and locally ordered, existing in a dynamic complex with protein partners. The interaction of the disordered Sic1 (a cyclin dependent kinase inhibitor) with Cdc4 (a component of an SCF ubiquitin ligase) involves the dynamic exchange of multiple linear binding motifs within Sic1 on and off of a single Cdc4 binding site. The disordered nature of the Sic1 chain enables Cdc4 to recognize multiply phosphorylated Sic1 by sensing a mean electrostatic field rather than only the field due to local binding of a linear motif. This sensitivity to multiple phosphorylations may facilitate a switch-like biological response of Sic1 ubiquitination and degradation to cyclin kinase activity. The regulatory (R) region of the cystic fibrosis transmembrane conductance regulator (CFTR) is another example, with transient and local ordering of multiple segments upon binding to multiple target proteins. The R region dynamic complex with the first nucleotide binding domain (NBD1) of CFTR appears to facilitate a rheostat-like function in activating CFTR channel conductance with an ability to integrate multiple regulatory binding inputs. We have measured NMR and SAXS structural data and used them as input to our program ENSEMBLE to generate sets of coordinates that represent significantly populated conformers within the isolated disordered states of Sic1 and the CFTR R region. The resulting ensembles can be docked to structures of the folded binding domains to further enable characterization of these dynamic complexes, leading to a better understanding of the role of disordered protein interactions in biological regulation." @default.
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- W2085405404 date "2009-02-01" @default.
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- W2085405404 title "Mechanisms Of Biological Regulation By Highly Dynamic Protein Complexes" @default.
- W2085405404 doi "https://doi.org/10.1016/j.bpj.2008.12.904" @default.
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