CHEBI:84624 - (Rp)-7-deaza-cAMPS

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ChEBI Name (Rp)-7-deaza-cAMPS ChEBI ID CHEBI:84624 ChEBI ASCII Name (Rp)-7-deaza-cAMPS Definition A nucleoside 3',5'-cyclic phosphorothioate having 7-deazaadenine as the nucleobase (the Rp-stereoisomer). Stars This entity has been manually annotated by the ChEBI Team. Submitter Margaret Duesbury Supplier Information No supplier information found for this compound. Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C11H13N4O5PS Net Charge 0 Average Mass 344.28300 Monoisotopic Mass 344.03443 InChI InChI=1S/C11H13N4O5PS/c12-9-5-1-2-15(10(5)14-4-13-9)11-7(16)8-6(19-11)3-18-21(17,22)20-8/h1-2,4,6-8,11,16H,3H2,(H,17,22)(H2,12,13,14)/t6-,7-,8-,11-,21-/m1/s1 InChIKey QINWOWYDYWBQQN-QOGDDWGYSA-N SMILES Nc1ncnc2n(ccc12)[C@@H]1O[C@@H]2CO[P@](S)(=O)O[C@H]2[C@H]1O ChEBI Ontology Outgoing (Rp)-7-deaza-cAMPS (CHEBI:84624) has functional parent tubercidin (CHEBI:48267) (Rp)-7-deaza-cAMPS (CHEBI:84624) is a N-glycosylpyrrolopyrimidine (CHEBI:48036) (Rp)-7-deaza-cAMPS (CHEBI:84624) is a nucleoside 3',5'-cyclic phosphorothioate (CHEBI:85287) IUPAC Name (2R,4aR,6R,7R,7aS)-6-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-7-hydroxy-2-sulfanyltetrahydro-2H,4H-2λ5-furo[3,2-d][1,3,2]dioxaphosphinin-2-one Synonyms Sources (Rp)-7-deazaadenosine-3',5'-cyclic monophosphorothioate ChEBI 7-deaza-Rp-cAMPS ChEBI Rp-7-CH-cAMPS ChEBI Citation Möller S, Alfieri A, Bertinetti D, Aquila M, Schwede F, Lolicato M, Rehmann H, Moroni A, Herberg FW (2014) Cyclic nucleotide mapping of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels. ACS chemical biology 9, 1128-1137 (Source: SUBMITTER) [PubMed:24605759] [show Abstract] Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels play a central role in the regulation of cardiac and neuronal firing rate, and these channels can be dually activated by membrane hyperpolarization and by binding of cyclic nucleotides. cAMP has been shown to directly bind HCN channels and modulate their activity. Despite this, while there are selective inhibitors that block the activation potential of the HCN channels, regulation by cAMP analogs has not been well investigated. A comprehensive screen of 47 cyclic nucleotides with modifications in the nucleobase, ribose moiety, and cyclic phosphate was tested on the three isoforms HCN1, HCN2, and HCN4. 7-CH-cAMP was identified to be a high affinity binder for HCN channels and crosschecked for its ability to act on other cAMP receptor proteins. While 7-CH-cAMP is a general activator for cAMP- and cGMP-dependent protein kinases as well as for the guanine nucleotide exchange factors Epac1 and Epac2, it displays the highest affinity to HCN channels. The molecular basis of the high affinity was investigated by determining the crystal structure of 7-CH-cAMP in complex with the cyclic nucleotide binding domain of HCN4. Electrophysiological studies demonstrate a strong activation potential of 7-CH-cAMP for the HCN4 channel in vivo. So, this makes 7-CH-cAMP a promising activator of the HCN channels in vitro whose functionality can be translated in living cells. Last Modified 23 March 2015