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BVLP is a Wellcome Trust Senior Investigator (Grant 101010).\nExport Date: 7 January 2020 \n Correspondence Address: Kühn, F.J.P.; Institute of Physiology, Medical Faculty, RWTH AachenGermany; email: fkuehn@ukaachen.de\nExport Date: 8 January 2020 \n Correspondence Address: Kühn, F.J.P.; Institute of Physiology, Medical Faculty, RWTH AachenGermany; email: fkuehn@ukaachen.de\nInstitute of Physiology, Medical Faculty, RWTH Aachen, Aachen, D52057, Germany \n Medicinal Chemistry and Drug Discovery, Department of Pharmacology, University of Oxford, Mansfield Road, Oxford, OX1 3QT, United Kingdom \n Wolfson Laboratory of Medicinal Chemistry, Department of Pharmacy and Pharmacology, University of Bath, Claverton Down, Bath, BA2 7AY, United Kingdom \n Cited By :7 \n Export Date: 1 July 2020 \n Correspondence Address: Kühn, F.J.P.; Institute of Physiology, Medical Faculty, RWTH AachenGermany; email: fkuehn@ukaachen.de \n Funding details: Deutsche Forschungsgemeinschaft, DFG, KU 2271/4-2 \n Funding text 1: The study was supported by the Deutsche Forschungsgemeinschaft (DFG, Grant KU 2271/4-2 to FJPK). 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The decisive binding site in NvTRPM2 is likely to be identical with the N-terminal ADPR binding pocket in zebra fish DrTRPM2. Our aim was a characterization of this binding site in NvTRPM2 with respect to its substrate specificity, in comparison to the classical ADPR interaction site within NUDT9H that is highly homologous in hTRPM2 and NvTRPM2, although only in NvTRPM2, catalytic (ADPRase) activity is conserved. With various ADPR analogues, key differences of the two sites were identified. Particularly, two reported antagonists on hTRPM2 were agonists on NvTRPM2. Moreover, IDP-ribose (IDPR) induced currents both in hTRPM2 and NvTRPM2 but not in NvTRPM2 mutants in which NUDT9H was absent. Thus, IDPR acts on NUDT9H rather than N-terminally, revealing a regulatory function of NUDT9H in NvTRPM2 opposed to that in hTRPM2. We propose that IDPR competitively inhibits the ADPRase function of NUDT9H and evokes ADPR accumulation. 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