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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2002-10-2
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-10785399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-10944333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-11032796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-11136860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-11747988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-11782420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-1721055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-1845962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-195942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-2153290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-2447936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-2542968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-2581780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-2842616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-2846074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-2999203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-6263632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-6276403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-6313664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-7630882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-8305078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-8703039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-9096404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-9163326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-9169501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-9210593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-9353302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-9433123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-9488681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12271124-9757107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13260-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12271124-3',5'-Cyclic-AMP Phosphodiesterases,
pubmed-meshheading:12271124-Amino Acid Motifs,
pubmed-meshheading:12271124-Amino Acid Sequence,
pubmed-meshheading:12271124-Animals,
pubmed-meshheading:12271124-Crystallography, X-Ray,
pubmed-meshheading:12271124-Cyclic AMP,
pubmed-meshheading:12271124-Cyclic GMP,
pubmed-meshheading:12271124-Cyclic Nucleotide Phosphodiesterases, Type 2,
pubmed-meshheading:12271124-Dimerization,
pubmed-meshheading:12271124-Dose-Response Relationship, Drug,
pubmed-meshheading:12271124-Mice,
pubmed-meshheading:12271124-Models, Biological,
pubmed-meshheading:12271124-Models, Molecular,
pubmed-meshheading:12271124-Molecular Sequence Data,
pubmed-meshheading:12271124-Protein Binding,
pubmed-meshheading:12271124-Protein Conformation,
pubmed-meshheading:12271124-Protein Structure, Quaternary,
pubmed-meshheading:12271124-Protein Structure, Tertiary,
pubmed-meshheading:12271124-Sequence Homology, Amino Acid
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pubmed:year |
2002
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pubmed:articleTitle |
The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding.
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pubmed:affiliation |
Departments of Pharmacology, and Biochemistry and Biological Structure, Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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