Fig. 2: Biochemical and structural characterization of novel CDHs.
From: A rational blueprint for the design of chemically-controlled protein switches
a Structural representation of CDH-2 composed of Bcl2 (beige surface) and LD3 (white cartoon) with the interfacial segment colored in green, the hotspot residues transplanted from the BH3 motif are shown in sticks. b SPR measurements of CDH-2 binding affinity. The dissociation constant determined for the interaction of Bcl2 with LD3 is 796 pM. c SPR drug competition assay determined the apparent IC50 of CDH-2 with Drug-2 around 67.5 nM. d Structural representation of CDH-3 composed of the mdm2 (purple surface):LD6 (white cartoon) complex with the interfacial segment colored in blue, the hotspot residues transplanted from the p53 are motif shown in sticks. e SPR measurements of CDH-3 binding affinity. The dissociation constant determined for the interaction of mdm2 with LD6 is 4.19 nM. f SPR drug competition assay determined the apparent IC50 of CDH-3 with Drug-3 around 106 nM. g The crystal structure of the CDH-3 consisting of the complex LD6 (pink tube) with mdm2 (purple surface) was in close agreement with the computational model of LD6 (gray tube) with complex with mdm2. h Transplanted hotspot residues in LD6 in sticks (pink) aligned with p53 peptide residues (teal) in a RMSD of 0.24 Å.
