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| {{STRUCTURE_1o7f| PDB=1o7f | SCENE= }} | | {{STRUCTURE_1o7f| PDB=1o7f | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE REGULATORY DOMAIN OF EPAC2'''
| | ===CRYSTAL STRUCTURE OF THE REGULATORY DOMAIN OF EPAC2=== |
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| ==Overview==
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| Cyclic adenosine monophosphate (cAMP) is a universal second messenger that, in eukaryotes, was believed to act only on cAMP-dependent protein kinase A (PKA) and cyclic nucleotide-regulated ion channels. Recently, guanine nucleotide exchange factors specific for the small GTP-binding proteins Rap1 and Rap2 (Epacs) were described, which are also activated directly by cAMP. Here, we have determined the three-dimensional structure of the regulatory domain of Epac2, which consists of two cyclic nucleotide monophosphate (cNMP)-binding domains and one DEP (Dishevelled, Egl, Pleckstrin) domain. This is the first structure of a cNMP-binding domain in the absence of ligand, and comparison with previous structures, sequence alignment and biochemical experiments allow us to delineate a mechanism for cyclic nucleotide-mediated conformational change and activation that is most likely conserved for all cNMP-regulated proteins. We identify a hinge region that couples cAMP binding to a conformational change of the C-terminal regions. Mutations in the hinge of Epac can uncouple cAMP binding from its exchange activity.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12469113}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12469113 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12469113}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Gef]] | | [[Category: Gef]] |
| [[Category: Regulation]] | | [[Category: Regulation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:28:46 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:21:38 2008'' |
