Fig. 1: Cryo-EM structures of MED23 and MED23Elk-1 complex.
From: Structural basis of human Mediator recruitment by the phosphorylated transcription factor Elk-1
a Elk-1 domains organization. Five domains of Elk-1 are indicated. ETS: DNA binding domain (in red); B: B-box responsible for association with SRF (in light gray); D and FQFP: D-box and FQFP docking sites for ERK (in green) and C-domain: TAD (in blue) that contains eight conserved S/T-P phosphoacceptor motifs. b MED23 domains organization. Boundaries of HEAT-repeat regions (HR1 to HR5) of MED23 are indicated. MED23 is fully folded with the exception of the last 30 amino acids indicated by a black dashed box. c Cryo-EM map of MED23 and (d) Cryo-EM map of MED23Elk-1 complex. e Map-model fit of Elk-1 (374–384) in surface representation at 2.6 sigma contour level. f Close-up view of MED23-Elk-1 (374–384) interface. In MED23, the Elk-1 binding site is formed by four helices: H19, H21 (from HR2) and H28, H30 (from HR3).
