Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Soluble guanylate cyclase.

Thomas L Poulos1

  • 1Department of Molecular Biology & Biochemistry, University of California Irvine, Irvine, CA 92697-3900, USA. poulos@uci.edu

Current Opinion in Structural Biology
|October 4, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

An assessment of the cytochrome P450 2-hydroxyisoflavanone synthase (2-HIS) crystal structure.

Communications biology·2026
Same author

Enhancement of Potency and Selectivity of 2-Aminoquinoline-Based Human Neuronal Nitric Oxide Synthase Inhibitors.

Journal of medicinal chemistry·2026
Same author

Potent, Selective, and Brain Penetrant Ether-Linked 2-Aminopyridine Inhibitors of Human Neuronal Nitric Oxide Synthase with Excellent Oral Bioavailability.

Journal of medicinal chemistry·2026
Same author

New Inhibitors of Neuronal Nitric Oxide Synthase for the Treatment of Melanoma.

Journal of medicinal chemistry·2026
Same author

Redox Partner Recognition and Selectivity of Cytochrome P450terp (CYP108A1).

Biochemistry·2025
Same author

Truncated pyridinylbenzylamines: Potent, selective, and highly membrane permeable inhibitors of human neuronal nitric oxide synthase.

Bioorganic & medicinal chemistry·2025
Same journal

Progress toward linking single-molecule behavior and condensate material properties.

Current opinion in structural biology·2026
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
See all related articles

Soluble guanylate cyclase (sGC) acts as a nitric oxide (NO) sensor. Its activation mechanism, involving NO binding and GTP cyclase activity, is illuminated by the crystal structure of prokaryotic sGC homologues.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Soluble guanylate cyclase (sGC) is a key mammalian sensor for nitric oxide (NO).
  • NO binding to sGC's heme group significantly enhances its GTP cyclase activity, producing cyclic GMP.
  • Cyclic GMP plays a crucial role in regulating various intracellular signaling pathways.

Purpose of the Study:

  • To elucidate the structure-function relationships within the sGC protein family.
  • To gain insights into the mechanism of sGC activation by nitric oxide.
  • To explore the structural basis of NO sensing and signal transduction.

Main Methods:

  • Analysis of the crystal structure of a prokaryotic sGC homologue.
  • Investigation of NO binding kinetics and equilibrium to sGC.

Related Experiment Videos

  • Elucidation of a proposed multistep mechanism for sGC activation.
  • Main Results:

    • The crystal structure of a prokaryotic sGC homologue provided novel insights into sGC protein family structure-function.
    • Understanding of NO binding to sGC, including its kinetics and equilibrium.
    • Evidence supporting a multistep activation mechanism involving at least two NO-binding sites.

    Conclusions:

    • The study provides critical structural information on sGC homologues, advancing our understanding of NO sensing.
    • Insights into the activation mechanism of sGC offer potential targets for therapeutic interventions.
    • Structural data on prokaryotic homologues are valuable for deciphering mammalian sGC function and regulation.