Fig. 5: Crystal structure of IDH1 R132Q bound to αKG and NADP-adducts are in closed and semi-closed conformations. | Nature Communications

Fig. 5: Crystal structure of IDH1 R132Q bound to αKG and NADP-adducts are in closed and semi-closed conformations.

From: Active site remodeling in tumor-relevant IDH1 mutants drives distinct kinetic features and potential resistance mechanisms

Fig. 5

In (A–C) and (E), a description of the ligands present is listed below each monomer. A R132Q:NADP(H):αKG:Ca2+/R132Q:NADP-αKG:Ca2+ dimer. Each R132Q monomer is highlighted using a slight change in color. B R132Q:NADP-αKG:Ca2+/ R132Q:NADP(H):αKG:Ca2+ dimer 1 (yellow) aligned with the dimer shown in (A) (magenta). C R132Q:NADP-αKG:Ca2+/R132Q:NADP(H):Ca2+ dimer 2 (orange) aligned with the dimer shown in (A) (magenta). D Monomer-based alignment of ICT- and αKG-containing R132Q monomers. E R132Q:NADP-TCEP:Ca2+/R132Q:NADP-TCEP:Ca2+ dimer. F Monomer-based alignment of adduct-containing R132Q monomers.

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