ArticleThe Journal of biological chemistry2016
Structural Basis of Cyclic Nucleotide Selectivity in cGMP-dependent Protein Kinase II.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Two new patients with acromesomelic dysplasia, PRKG2 type-identification and characterization of the first missense variant.European journal of human genetics : EJHG · 2024Article
- Cyclic nucleotide selectivity of protein kinase G isozymes.Protein science : a publication of the Protein Society · 2021Review
- Identification of Novel Substrates for cGMP Dependent Protein Kinase (PKG) through Kinase Activity Profiling to Understand Its Putative Role in Inherited Retinal Degeneration.International journal of molecular sciences · 2021Article
- CUTie2: The Attack of the Cyclic Nucleotide Sensor Clones.Frontiers in molecular biosciences · 2021Article
- Active PKG II inhibited the growth and migration of ovarian cancer cells through blocking Raf/MEK and PI3K/Akt signaling pathways.Bioscience reports · 2019Article
- Structures of the cGMP-dependent protein kinase in malaria parasites reveal a unique structural relay mechanism for activation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Neutron Crystallography Detects Differences in Protein Dynamics: Structure of the PKG II Cyclic Nucleotide Binding Domain in Complex with an Activator.Biochemistry · 2018Article
- Protein Kinases Type II (PKG II) Combined with L-Arginine Significantly Ameliorated Xenograft Tumor Development: Is L-Arginine a Potential Alternative in PKG II Activation?Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- Switching Cyclic Nucleotide-Selective Activation of Cyclic Adenosine Monophosphate-Dependent Protein Kinase Holoenzyme Reveals Distinct Roles of Tandem Cyclic Nucleotide-Binding Domains.ACS chemical biology · 2017Article
- Structural Basis of Analog Specificity in PKG I and II.ACS chemical biology · 2017Article
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Authors and funding
12 authors at 8 institutions in 4 countries.
Funding
Abstract
Membrane-bound cGMP-dependent protein kinase (PKG) II is a key regulator of bone growth, renin secretion, and memory formation. Despite its crucial physiological roles, little is known about its cyclic nucleotide selectivity mechanism due to a lack of structural information. Here, we find that the C-terminal cyclic nucleotide binding (CNB-B) domain of PKG II binds cGMP with higher affinity and selectivity when compared with its N-terminal CNB (CNB-A) domain. To understand the structural basis of cGMP selectivity, we solved co-crystal structures of the CNB domains with cyclic nucleotides. Our structures combined with mutagenesis demonstrate that the guanine-specific contacts at Asp-412 and Arg-415 of the αC-helix of CNB-B are crucial for cGMP selectivity and activation of PKG II. Structural comparison with the cGMP selective CNB domains of human PKG I and Plasmodium falciparum PKG (PfPKG) shows different contacts with the guanine moiety, revealing a unique cGMP selectivity mechanism for PKG II.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.