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. 2020 Feb 19;11:956. doi: 10.1038/s41467-020-14750-x

Fig. 8. XL-MS confirms the repressive helix 12 conformation within the orthosteric ligand-binding pocket.

Fig. 8

a Distances between K474 on helix 12 and several lysine residues structurally proximal to helix 12 (K265 and K275) or further away (K301 and K457) in the crystal structure of PPARγ LBD bound to T0070907 and NCoR ID2 peptide (PDB 6ONI). b Relative peak area of four K474-crosslinked peptides normalized to a control uncrosslinked peptide and to the highest mean peak area within each condition (mean ± s.e.m.; n = 3). Source data are provided as a Source Data file.