Backbone and side chain NMR assignments of the H-NOX domain from Nostoc sp. in complex with BAY58-2667 (cinaciguat)

Garyfallia I. Makrynitsa, Aikaterini I. Argyriou, Georgios Dalkas, Dimitra A. Georgopoulou, Marina Bantzi, Athanassios Giannis, Andreas Papapetropoulos, Georgios A. Spyroulias

Research output: Contribution to journalArticlepeer-review

Abstract

Soluble guanylate cyclase (sGC) enzyme is activated by the gaseous signaling agent nitric oxide (NO) and triggers the conversion of GTP (guanosine 5′-triphosphate) to cGMP (cyclic guanylyl monophosphate). It contains the heme binding H-NOX (heme-nitric oxide/oxygen binding) domain which serves as the sensor of NO and it is highly conserved across eukaryotes and bacteria as well. Many research studies focus on the synthesis of chemical compounds bearing possible therapeutic action, which mimic the heme moiety and activate the sGC enzyme. In this study, we report a preliminary solution NMR (Nuclear Magnetic Resonance) study of the H-NOX domain from Nostoc sp. cyanobacterium in complex with the chemical sGC activator cinaciguat (BAY58-2667). An almost complete sequence-specific assignment of its 1H, 15N and 13C resonances was obtained and its secondary structure predicted by TALOS+.

Original languageEnglish (US)
JournalBiomolecular NMR Assignments
DOIs
StateAccepted/In press - 2020

Keywords

  • BAY58-2667
  • Cinaciguat
  • H-NOX domain
  • NMR spectroscopy
  • Soluble guanylate cyclase (sGC)

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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