Fig. 4

Ligand dependency of SRC1 RID binding to the VDRRXRα heterodimer AF2 surface. Schematic representations illustrate differential experiments of VDRRXRα: ligand: DNA complex verse VDRRXRα: ligand: DNA: SRC1 RID complex (on the left). Differential HDX data are mapped onto the surface of VDRRXR heterodimer structure model in the presence and absence of SRC1 RID (on the right). a Conformational changes of VDRRXRα: 1,25D3: DR3 complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xi)). b Conformational changes of VDRRXRα: 1,25D3: DR3 half-site complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xii)). c Conformational changes of VDRRXRα: Cmpd1: DR3 complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xiii)). d Conformational changes of VDRRXRα: Cmpd1: DR3 half-site complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xiv)). e Conformational changes of VDRRXRα: Cmpd2: DR3 complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xv)). f Conformational changes of VDRRXRα: Cmpd2: DR3 half-site complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xvi)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; black, DNA VBSs