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Domain-Specific Agonist Binding Affinities Explain Structural and Functional Regulation of TRPM2

2026-04-01

Abstract excerpt

TRPM2 is a Ca²⁺-permeable cation channel activated by ADP-ribose (ADPR) and oxidative stress, yet the relative contributions of its two nucleotide-binding domains, MHR1/2 and NUDT9H, remain incompletely understood. Here, we quantitatively determine the affinities of the isolated human TRPM2 MHR1/2 and NUDT9H domains for ADPR, 2’-deoxy-dADPR (dADPR), and 8-Br-cADPR using biophysical approaches. The MHR1/2 domain bi...

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Identifiers and source

Literature Corpus work
9f05378b-a409-5068-a730-84d4b9d5f194
DOI
10.64898/2026.03.30.715250
Open publication

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Domain-Specific Agonist Binding Affinities Explain Structural and Functional Regulation of TRPM2DOI 10.64898/2026.03.30.715250
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