What question did this study set out to answer?

The study aims to explore how a sulfur-modified cyclic dinucleotide analog affects the inhibition of phosphodiesterase in Mycobacterium tuberculosis.

April 16, 2026Open Access

Structural and biochemical insights into the inhibition of Mycobacterium tuberculosis cyclic dinucleotide phosphodiesterase by a sulfur-modified cyclic dinucleotide analog

DHDagur Singh HanumanIndian Institute of Chemical Technology SNSingh NeeharikaIndian Institute of Chemical Technology SMSinha Krishna Murari

Key Points

The study aims to explore how a sulfur-modified cyclic dinucleotide analog affects the inhibition of phosphodiesterase in Mycobacterium tuberculosis.
Biochemical assays to assess binding interactions
Structural analysis of enzyme-inhibitor complexes
Evaluation of catalytic activity changes
ES-cAAMP binds to Mycobacterium tuberculosis CdnP with a unique horseshoe conformation
Inhibition occurs by competing with the substrate
CdnP's catalytic activity significantly decreases when bound to the analog

Abstract

ES-cAAMP binds to Mtb CdnP in a unique horseshoe conformation in the catalytic pocket (CG-site) away from the catalytic cation and residues, which are in the R-site. It competes with the substrate and inhibits CdnP's catalytic activity.

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Cite This Study

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

synapsesocial.com/papers/69e07d1d2f7e8953b7cbe336 https://doi.org/https://doi.org/10.1039/d6cb00006a

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