Fig. 3: Crystal structure of NADP(H)-bound IDH1 R132Q shows a typical open conformation. | Nature Communications

Fig. 3: Crystal structure of NADP(H)-bound IDH1 R132Q shows a typical open conformation.

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

Fig. 3

A The binary R132Q:NADP(H) complex is shown with each monomer highlighted using a slight color change. B Dimer-based alignments of R132Q:NADP(H) (red), WT:NADP(H)13 (black), and R132H:NADP(H) (light green)30. C Monomer-based alignments of the structures in (B). D The view show in (C) was simplified to highlight catalytic residues Y139 and K212 (though the latter residue drives catalysis in the monomer not shown as this is a monomer-based alignment), residue R132(H/Q), and the cofactor.

Back to article page