Fig. 5: Mat1 binds tightly to Cdk7/Cyclin H and synergizes with Cdk7 T-loop phosphorylation to stabilize the tripartite complex.
From: Structural basis of Cdk7 activation by dual T-loop phosphorylation
a, b Multi-cycle kinetics of SPR measurements. For analysis, Cdk7/Cyclin H complex was used as analyte in a serial 1:3 dilution ranging from 150 nM to 0.2 nM (left panels). Dissociation constants were calculated by determination of the steady-state affinity (right panels). c Thermal stability of Cdk7 complexes was determined at a protein concentration of 2.5 µM in storage buffer (20 mM Hepes pH7.6, 150 mM NaCl, 1 mM TCEP) by monitoring intrinsic fluorescence at 350 and 330 nm with a nanoDSF device (NanoTemper). The chromatogram shows the melting curves of the ternary complexes indicated. d Dotplot representation of the melting point (Tm) of binary and ternary Cdk7 preparations. Stability was monitored in triplicate (samples w/o Mat1 and with Mat11-309) or comprising twelve (S_T), nine (A_pT) and eleven (pS_pT) replicates (samples with Mat1230-309). Data represent mean ± SD. Source data are provided as a Source Data file.
