Binding Rate Constants Reveal Distinct Features of Disordered Protein Domains
Intrinsically Disordered Proteins
CREB-binding protein
DOI:
10.1021/acs.biochem.5b00520
Publication Date:
2015-07-08T04:07:33Z
AUTHORS (4)
ABSTRACT
Intrinsically disordered proteins (IDPs) are abundant in the proteome and involved key cellular functions. However, experimental data about binding kinetics of IDPs as a function different environmental conditions scarce. We have performed an extensive characterization ionic strength dependence interaction between molten globular nuclear co-activator domain (NCBD) CREB protein five ligands, including intrinsically activation p160 transcriptional co-activators (SRC1, TIF2, ACTR), p53 transactivation domain, folded pointed (PNT) transcription factor ETS-2. Direct comparisons rate constants under identical show that association constant, kon, for interactions NCBD domains is high at low salt concentrations (90-350 × 10(6) M(-1) s(-1) 4 °C) but reduced significantly (10-30-fold) with increasing reaches plateau around physiological strength. In contrast, kon PNT only 7 (4 °C salt) displays weak dependence, which could reflect distinctly relies less on electrostatic interactions. Furthermore, basal constant (in absence interactions) interactions, exceeding those typically observed proteins. One likely interpretation large number possible collisions leading to productive on-pathway encounter complex, while more restricted terms orientation. Our results highlight importance involving emphasize significance studies compare properties ordered
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