TY - JOUR
T1 - Backbone and side chain NMR assignments of the H-NOX domain from Nostoc sp. in complex with BAY58-2667 (cinaciguat)
AU - Makrynitsa, Garyfallia I.
AU - Argyriou, Aikaterini I.
AU - Dalkas, Georgios
AU - Georgopoulou, Dimitra A.
AU - Bantzi, Marina
AU - Giannis, Athanassios
AU - Papapetropoulos, Andreas
AU - Spyroulias, Georgios A.
N1 - Publisher Copyright:
© 2020, Springer Nature B.V.
PY - 2021/4
Y1 - 2021/4
N2 - 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+.
AB - 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+.
KW - BAY58-2667
KW - Cinaciguat
KW - H-NOX domain
KW - NMR spectroscopy
KW - Soluble guanylate cyclase (sGC)
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UR - http://www.scopus.com/inward/citedby.url?scp=85094636579&partnerID=8YFLogxK
U2 - 10.1007/s12104-020-09982-3
DO - 10.1007/s12104-020-09982-3
M3 - Article
C2 - 33128204
AN - SCOPUS:85094636579
SN - 1874-2718
VL - 15
SP - 53
EP - 57
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
IS - 1
ER -