Works (1)
Updated: July 5th, 2023 15:48
2010 journal article
Kinetic Stability May Determine the Interaction Dynamics of the Bifunctional Protein DCoH1, the Dimerization Cofactor of the Transcription Factor HNF-1 alpha
BIOCHEMISTRY, 49(47), 10187–10197.
MeSH headings : Chromatography, Gel; Enzyme Stability; Guanidine / pharmacology; Hepatocyte Nuclear Factor 1-alpha / metabolism; Hydro-Lyases / genetics; Hydro-Lyases / metabolism; Kinetics; Models, Molecular; Point Mutation; Protein Denaturation; Protein Multimerization; Protein Unfolding; Spectrometry, Fluorescence; Tryptophan / chemistry
TL;DR:
This work shows that a point mutation at the DCoH1 tetramer interface, Thr 51 Ser, overcomes the dissociation barrier of the homotetramer and increases the interaction with HNF-1α, and proposes an unfolding pathway in which the tetramer unfolds slowly, but the dimer folds reversibly.
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Added: August 6, 2018
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