Role of the Coiled-Coil Domain in Allosteric Activity Regulation in Soluble Guanylate Cyclase.

ABSTRACT: Soluble guanylate cyclase (sGC) is the primary nitric oxide (NO) receptor in higher eukaryotes, including humans. NO-dependent signaling via sGC is associated with important physiological effects in the vascular, pulmonary, and neurological systems, and sGC itself is an established drug target for the treatment of pulmonary hypertension due to its central role in vasodilation. Despite isolation in the late 1970s, high-resolution structural information on full-length sGC remained elusive until recent cryo-electron microscopy structures were determined of the protein in both the basal unactivated state and the NO-activated state. These structures revealed large-scale conformational changes upon activation that appear to be centered on rearrangements within the coiled-coil (CC) domains in the

SUBMITTER: Wittenborn EC 

PROVIDER: S-EPMC10686098 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature