| Literature DB >> 24090476 |
Margarete von Wantoch Rekowski1, Vijay Kumar2, Focco van den Akker2, Athanassios Giannis1, Andreas Papapetropoulos3, Zongmin Zhou3,4, Johann Moschner1, Antonia Marazioti3, Marina Bantzi1, Georgios A Spyroulias3.
Abstract
Recently, 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 αF helix containing 110-114 residues contributes to the higher activation triggered by 20.Entities:
Mesh：
Substances：
Year: 2013 PMID： 24090476 PMCID： PMC3902542 DOI： 10.1021/jm400539d
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446