Solution Structure of the cGMP Binding GAF Domain from Phosphodiesterase 5: Insights into Nucleotide Specificity, Dimerization, and cGMP-Dependent Conformational Change

August 15, 2008

Journal Article

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.

Revised: April 7, 2011 | Published: August 15, 2008

Citation

Heikaus C.C., J.R. Stout, M.R. Sekharan, C.M. Eakin, P. Rajagopal, P.S. Brzovic, and J.A. Beavo, et al. 2008. "Solution Structure of the cGMP Binding GAF Domain from Phosphodiesterase 5: Insights into Nucleotide Specificity, Dimerization, and cGMP-Dependent Conformational Change." Journal of Biological Chemistry 283, no. 33:22749-22759. doi:10.1074/jbc.M801577200