1o7f

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[[Image:1o7f.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1o7f", creates the "Structure Box" on the page.
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{{STRUCTURE_1o7f| PDB=1o7f | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7f OCA], [http://www.ebi.ac.uk/pdbsum/1o7f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o7f RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE REGULATORY DOMAIN OF EPAC2'''
'''CRYSTAL STRUCTURE OF THE REGULATORY DOMAIN OF EPAC2'''
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[[Category: Wittinghofer, A.]]
[[Category: Wittinghofer, A.]]
[[Category: Wolf, E.]]
[[Category: Wolf, E.]]
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[[Category: camp]]
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[[Category: Camp]]
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[[Category: camp-gef2]]
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[[Category: Camp-gef2]]
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[[Category: campb binding doamin]]
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[[Category: Campb binding doamin]]
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[[Category: epac2]]
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[[Category: Epac2]]
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[[Category: exchange factor]]
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[[Category: Exchange factor]]
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[[Category: gef]]
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[[Category: Gef]]
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[[Category: regulation]]
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[[Category: Regulation]]
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Revision as of 00:28, 3 May 2008

Image:1o7f.jpg

Template:STRUCTURE 1o7f

CRYSTAL STRUCTURE OF THE REGULATORY DOMAIN OF EPAC2


Overview

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.

About this Structure

1O7F is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure and regulation of the cAMP-binding domains of Epac2., Rehmann H, Prakash B, Wolf E, Rueppel A, de Rooij J, Bos JL, Wittinghofer A, Nat Struct Biol. 2003 Jan;10(1):26-32. PMID:12469113 Page seeded by OCA on Sat May 3 03:28:46 2008

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