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Crystal structure of a new sGC activator (analogue of BAY 58-2667) bound to nostoc H-NOX domainCrystal structure of a new sGC activator (analogue of BAY 58-2667) bound to nostoc H-NOX domain
Structural highlights
Publication Abstract from PubMedRecently, the structure of BAY 58-2667 bound to the Nostoc sp. H-NOX domain was published. On the basis of this structural information, we designed BAY 58-2667 derivatives and tested their effects on soluble guanylyl cyclase (sGC) activity. Derivative 20 activated sGC 4.8-fold more than BAY 58-2667. Co-crystallization of 20 with the Ns H-NOX domain revealed that the increased conformational distortion at the C-terminal region of alphaF helix containing 110-114 residues contributes to the higher activation triggered by 20. Insights into Soluble Guanylyl Cyclase Activation Derived from Improved Heme-Mimetics.,von Wantoch Rekowski M, Kumar V, Zhou Z, Moschner J, Marazioti A, Bantzi M, Spyroulias GA, van den Akker F, Giannis A, Papapetropoulos A J Med Chem. 2013 Oct 24. PMID:24090476[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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