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

Dagur Singh Hanuman; Singh Neeharika; Sinha Krishna Murari; Simpa K. Yeboah; Herman O. Sintim; Eerappa Rajakumara

doi:10.1039/d6cb00006a

January 1, 2026RSC Chemical BiologyOpen Access

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

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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

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Implication

This research demonstrates the inhibition of Mycobacterium tuberculosis enzyme activity by a sulfur-modified cyclic dinucleotide analog, indicating potential therapeutic insights.

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Cite This Study

Hanuman et al. (2026) studied this question.

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

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

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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