1MC0

Regulatory Segment of Mouse 3',5'-Cyclic Nucleotide Phosphodiesterase 2A, Containing the GAF A and GAF B Domains

Summary for 1MC0

• Entry DOI: 10.2210/pdb1mc0/pdb
• Descriptor: 3',5'-cyclic nucleotide phosphodiesterase 2A, CYCLIC GUANOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: gaf domain, 3', 5'-cyclic nucleotide phosphodiesterase, 5'-guanosine monophosphate, hydrolase
• Biological source: Mus musculus (house mouse)
• Cellular location: Membrane; Peripheral membrane protein (Potential): Q922S4
• Total number of polymer chains: 1
• Total formula weight: 41769.12

Authors

Martinez, S.,Wu, A.,Glavas, N.,Tang, X.,Turley, S.,Hol, W.,Beavo, J. (deposition date: 2002-08-04, release date: 2002-10-02, Last modification date: 2024-11-13)

Primary citation

Martinez, S.E.,Wu, A.Y.,Glavas, N.A.,Tang, X.B.,Turley, S.,Hol, W.G.,Beavo, J.A.
The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding.
Proc.Natl.Acad.Sci.USA, 99:13260-13265, 2002

PubMed Abstract: Cyclic nucleotide phosphodiesterases (PDEs) regulate all pathways that use cGMP or cAMP as a second messenger. Five of the 11 PDE families have regulatory segments containing GAF domains, 3 of which are known to bind cGMP. In PDE2 binding of cGMP to the GAF domain causes an activation of the catalytic activity by a mechanism that apparently is shared even in the adenylyl cyclase of Anabaena, an organism separated from mouse by 2 billion years of evolution. The 2.9-A crystal structure of the mouse PDE2A regulatory segment reported in this paper reveals that the GAF A domain functions as a dimerization locus. The GAF B domain shows a deeply buried cGMP displaying a new cGMP-binding motif and is the first atomic structure of a physiological cGMP receptor with bound cGMP. Moreover, this cGMP site is located well away from the region predicted by previous mutagenesis and structural genomic approaches.

PubMed: 12271124
DOI: 10.1073/pnas.192374899

Experimental method

X-RAY DIFFRACTION (2.86 Å)