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February 26, 2026Physical Chemistry Chemical Physics1 citations

Discovery of a new binding site for the possible gain in neomorphic activity in R132HIDH1

NNNandeshwar NandeshwarIndian Institute of Technology Dhanbad ABAbhipsa Sekhar BiswalIndian Institute of Technology Dhanbad SCSoumit ChatterjeeIndian Institute of Technology Dhanbad

Key Points

To identify a new binding site associated with neomorphic activity in the R132H_IDH1 variant.
Characterization of IDH1 catalytic activity in vitro
Biochemical assays to assess binding affinity
Structural analysis using X-ray crystallography
Discovery of a novel binding site that enhances neomorphic activity
Increased catalytic efficiency observed in the R132H_IDH1 variant
Potential implications for targeted therapies in related diseases

Abstract

In the Krebs cycle, the isocitrate dehydrogenase 1 (IDH1) catalyses the conversion of isocitrate (ICT) to α-ketoglutarate (α-KG), generating Nicotinamide Adenine Dinucleotide Phosphate (NADPH), which helps maintain redox balance, facilitates...

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Discovery of a new binding site for the possible gain in neomorphic activity in R132HIDH1 | Synapse

Cite This Study

Nandeshwar et al. (Thu,) studied this question.

synapsesocial.com/papers/699fe34695ddcd3a253e705e https://doi.org/https://doi.org/10.1039/d5cp04261e