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. 2014 Jul 7;289(34):23449–23464. doi: 10.1074/jbc.M114.585539

FIGURE 9.

FIGURE 9.

DR1 substitutions away from the DM-binding site and pocket 1 alter DM susceptibility. A, mutated positions are indicated on ribbon diagram of DR1 bound to peptide A2(104–117) (gray, PDB code 1AQD) (31) or DR1 bound to DM (green, PDB code 4FQX) (24). Positions of P1 and P9 pockets in DR1-peptide complex and sites of DM interaction in DR1-DM complex are indicated. B–E, DM binding of CLIP-peptide complexes of wild-type DR1 (B), H33S,A37K (C), P16Y,Q18K (D), and T41A (E) as measured by SPR. F, DM susceptibility of CLIP bound to wild-type and mutant DR1 with wild-type and P95A DM. G, region around DR1 αThr-41, αTrp-43, and extended strand region shown for structure of DR1-A1L9. H, same region shown for structure of DR1 bound to DM (24). I, dissociation of CLIP peptide complexes of WT and T41A DR1 in the presence of various concentrations of WT and P95A DM. J, binding of WT and P95A DM to immobilized DO measured by bio-layer interferometry. K, dissociation kinetics were measured wild-type DR1 and T41A mutant bound to WT, A1, and A1L9 peptides, with DM susceptibility summarized in L.