Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases

PADAYATTI, P

doi:10.1016/j.pharmthera.2004.08.003

Cited by 50Receptor Mechanisms and SignalingPhosphodiesterase function and regulationProtein Kinase Regulation and GTPase Signaling

Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases

PADAYATTI, P·2004·Pharmacology & Therapeutics

DOI 10.1016/j.pharmthera.2004.08.003

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Abstract

Guanylyl cyclases (GC) are proteins that are essential for the production of the second messenger cyclic guanosine monophosphate (cGMP). Mammalian GC have attracted considerable interest due to their roles in important physiological processes such as vasodilation, vision, and bone growth. In addition, their link to disease and concomitant pharmaceutical potential have made these cyclases a long standing target for probing their intriguing mechanism of activation with the aim of drug development. The vasodilatory drugs nitroglycerin and nesiritide act through (different) GC pathways and have both been shown to provide beneficial relief for congestive heart failure patients. New structural insights are recently emerging on the activation mechanism and regulation of these receptors. The aim of this review is to discuss the interesting differences and similarities between members of the soluble and membrane bound GC in detail and put these in context with the structural knowledge that is available to date. These efforts contribute to an enhanced understanding of the GC and will likely lead to an increased success in structure-based therapeutic intervention.

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Inhibition by guanosine cyclic monophosphate (cGMP) analogues of uptake of [3H]3′,5′-cGMP without stimulation of ATPase activity in human erythrocyte inside-out vesicles11Abbreviations: 3′,5′-cGMP, guanosine 3′,5′-cyclic monophosphate; 2′,3′-cGMP, guanosine 2′,3′-cyclic monophosphate; N-mb-cGMP, N2-monobutyryl guanosine 3′,5′-cyclic monophosphate; O-mb-cGMP, 2′-O-monobutyryl guanosine 3′,5′-cyclic monophosphate; Db-cGMP, N2,2′-O-dibutyryl guanosine 3′,5′-cyclic monophosphate; Br-cGMP, 8′-bromo guanosine 3′,5′-cyclic monophosphate; Rp-cGMPS, Rp-monophosphorothioate guanosine 3′,5′-cyclic monophosphate; Sp-cGMPS, Sp-monophosphorothioate guanosine 3′,5′-cyclic monophosphate; 3′,5′-cAMP, Adenosine 3′,5′-cyclic monophosphate; and MRP, multidrug resistance protein.
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Authors: PADAYATTI, P.
Affiliations: Case Western Reserve University (US)
Corresponding author: PADAYATTI, P
ORCID: PADAYATTI, P
Venue: Pharmacology & Therapeutics
Publisher: Elsevier BV
Published: 2004-11
Volume: 104
Issue: 2
Pages: 83-99
ISSN: 0163-7258 (ISSN-L)
DOI: 10.1016/j.pharmthera.2004.08.003
OpenAlex: W1990355822
Cited by: 50
References: 163
Citations by year: 2024: 2 · 2023: 1 · 2022: 3 · 2018: 2 · 2016: 1 · 2015: 4 · 2013: 3 · 2012: 3
FWCI: 2.49
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Pharmacology & Therapeutics (publishedVersion)
PubMed (publishedVersion)
Funders: American Heart Association
National Institutes of Health
National Institute of Diabetes and Digestive and Kidney Diseases (R21DK065066)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Phosphodiesterase function and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: guanylate cyclase, cyclic GMP, enzyme activation mechanism, soluble guanylate cyclase, nitric oxide signaling, nitroglycerin, nesiritide, congestive heart failure, structure-based drug design, vasodilation
MeSH terms: Receptors, Enterotoxin, Atrial Natriuretic Factor Receptor B, Animals, Cyclic GMP, Guanylate Cyclase, Humans, Protein Binding, Protein Structure, Tertiary, Receptors, Atrial Natriuretic Factor, Receptors, Peptide, Receptors, Guanylate Cyclase-Coupled

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Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases

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