skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: 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}
}