Structural Perspectives on the Mechanism of Soluble Guanylate Cyclase Activation.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
21 May 2021
Historique:
received: 03 05 2021
revised: 17 05 2021
accepted: 18 05 2021
entrez: 2 6 2021
pubmed: 3 6 2021
medline: 17 6 2021
Statut: epublish

Résumé

The enzyme soluble guanylate cyclase (sGC) is the prototypical nitric oxide (NO) receptor in humans and other higher eukaryotes and is responsible for transducing the initial NO signal to the secondary messenger cyclic guanosine monophosphate (cGMP). Generation of cGMP in turn leads to diverse physiological effects in the cardiopulmonary, vascular, and neurological systems. Given these important downstream effects, sGC has been biochemically characterized in great detail in the four decades since its discovery. Structures of full-length sGC, however, have proven elusive until very recently. In 2019, advances in single particle cryo-electron microscopy (cryo-EM) enabled visualization of full-length sGC for the first time. This review will summarize insights revealed by the structures of sGC in the unactivated and activated states and discuss their implications in the mechanism of sGC activation.

Identifiants

pubmed: 34064029
pii: ijms22115439
doi: 10.3390/ijms22115439
pmc: PMC8196705
pii:
doi:

Substances chimiques

Nitric Oxide 31C4KY9ESH
Soluble Guanylyl Cyclase EC 4.6.1.2
Cyclic GMP H2D2X058MU

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM127854
Pays : United States
Organisme : NIH HHS
ID : GM127854
Pays : United States

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Auteurs

Elizabeth C Wittenborn (EC)

California Institute for Quantitative Biosciences, Departments of Chemistry and of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

Michael A Marletta (MA)

California Institute for Quantitative Biosciences, Departments of Chemistry and of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

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