Solution Structure of the cGMP Binding GAF Domain from Phosphodiesterase 5: Insights into Nucleotide Specificity, Dimerization, and cGMP-Dependent Conformational Change
Abstract
Phosphodiesterase 5 (PDE5) controls intracellular levels of cGMP through its regulation of cGMP hydrolysis. Hydrolytic activity of the C-terminal catalytic domain is increased by cGMP binding to the N-terminal GAF A domain. We present the NMR solution structure of the cGMP-bound PDE5A GAF A domain. The cGMP orientation in the buried binding pocket was defined through 37 intermolecular NOEs.
- Authors:
- Publication Date:
- Research Org.:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 937368
- DOE Contract Number:
- AC05-76RL01830
- Resource Type:
- Journal Article
- Journal Name:
- Journal of Biological Chemistry, 283(33):22749-22759
- Additional Journal Information:
- Journal Volume: 283; Journal Issue: 33; Journal ID: ISSN 0021-9258
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; CONFORMATIONAL CHANGES; DIMERIZATION; HYDROLYSIS; NUCLEOTIDES; ORIENTATION; PHOSPHODIESTERASES; REGULATIONS; SPECIFICITY; Environmental Molecular Sciences Laboratory
Citation Formats
Heikaus, Clemens C, Stout, Joseph R, Sekharan, Monica R, Eakin, Catherine M, Rajagopal, Ponni, Brzovic, Peter S, Beavo, Joseph A, and Klevit, Rachel E. Solution Structure of the cGMP Binding GAF Domain from Phosphodiesterase 5: Insights into Nucleotide Specificity, Dimerization, and cGMP-Dependent Conformational Change. United States: N. p., 2008.
Web. doi:10.1074/jbc.M801577200.
Heikaus, Clemens C, Stout, Joseph R, Sekharan, Monica R, Eakin, Catherine M, Rajagopal, Ponni, Brzovic, Peter S, Beavo, Joseph A, & Klevit, Rachel E. Solution Structure of the cGMP Binding GAF Domain from Phosphodiesterase 5: Insights into Nucleotide Specificity, Dimerization, and cGMP-Dependent Conformational Change. United States. https://doi.org/10.1074/jbc.M801577200
Heikaus, Clemens C, Stout, Joseph R, Sekharan, Monica R, Eakin, Catherine M, Rajagopal, Ponni, Brzovic, Peter S, Beavo, Joseph A, and Klevit, Rachel E. 2008.
"Solution Structure of the cGMP Binding GAF Domain from Phosphodiesterase 5: Insights into Nucleotide Specificity, Dimerization, and cGMP-Dependent Conformational Change". United States. https://doi.org/10.1074/jbc.M801577200.
@article{osti_937368,
title = {Solution Structure of the cGMP Binding GAF Domain from Phosphodiesterase 5: Insights into Nucleotide Specificity, Dimerization, and cGMP-Dependent Conformational Change},
author = {Heikaus, Clemens C and Stout, Joseph R and Sekharan, Monica R and Eakin, Catherine M and Rajagopal, Ponni and Brzovic, Peter S and Beavo, Joseph A and Klevit, Rachel E},
abstractNote = {Phosphodiesterase 5 (PDE5) controls intracellular levels of cGMP through its regulation of cGMP hydrolysis. Hydrolytic activity of the C-terminal catalytic domain is increased by cGMP binding to the N-terminal GAF A domain. We present the NMR solution structure of the cGMP-bound PDE5A GAF A domain. The cGMP orientation in the buried binding pocket was defined through 37 intermolecular NOEs.},
doi = {10.1074/jbc.M801577200},
url = {https://www.osti.gov/biblio/937368},
journal = {Journal of Biological Chemistry, 283(33):22749-22759},
issn = {0021-9258},
number = 33,
volume = 283,
place = {United States},
year = {Fri Aug 15 00:00:00 EDT 2008},
month = {Fri Aug 15 00:00:00 EDT 2008}
}
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