2byv: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2byv.gif|left|200px]] | [[Image:2byv.gif|left|200px]] | ||
'''STRUCTURE OF THE CAMP RESPONSIVE EXCHANGE FACTOR EPAC2 IN ITS AUTO-INHIBITED STATE''' | {{Structure | ||
|PDB= 2byv |SIZE=350|CAPTION= <scene name='initialview01'>2byv</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF THE CAMP RESPONSIVE EXCHANGE FACTOR EPAC2 IN ITS AUTO-INHIBITED STATE''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2BYV is a [ | 2BYV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BYV OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state., Rehmann H, Das J, Knipscheer P, Wittinghofer A, Bos JL, Nature. 2006 Feb 2;439(7076):625-8. PMID:[http:// | Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state., Rehmann H, Das J, Knipscheer P, Wittinghofer A, Bos JL, Nature. 2006 Feb 2;439(7076):625-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16452984 16452984] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 26: | Line 35: | ||
[[Category: regulation]] | [[Category: regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:08:32 2008'' | ||
Revision as of 17:08, 20 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE CAMP RESPONSIVE EXCHANGE FACTOR EPAC2 IN ITS AUTO-INHIBITED STATE
OverviewOverview
Epac proteins (exchange proteins directly activated by cAMP) are guanine-nucleotide-exchange factors (GEFs) for the small GTP-binding proteins Rap1 and Rap2 that are directly regulated by the second messenger cyclic AMP and function in the control of diverse cellular processes, including cell adhesion and insulin secretion. Here we report the three-dimensional structure of full-length Epac2, a 110-kDa protein that contains an amino-terminal regulatory region with two cyclic-nucleotide-binding domains and a carboxy-terminal catalytic region. The structure was solved in the absence of cAMP and shows the auto-inhibited state of Epac. The regulatory region is positioned with respect to the catalytic region by a rigid, tripartite beta-sheet-like structure we refer to as the 'switchboard' and an ionic interaction we call the 'ionic latch'. As a consequence of this arrangement, the access of Rap to the catalytic site is sterically blocked. Mutational analysis suggests a model for cAMP-induced Epac activation with rigid body movement of the regulatory region, the features of which are universally conserved in cAMP-regulated proteins.
About this StructureAbout this Structure
2BYV is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state., Rehmann H, Das J, Knipscheer P, Wittinghofer A, Bos JL, Nature. 2006 Feb 2;439(7076):625-8. PMID:16452984
Page seeded by OCA on Thu Mar 20 16:08:32 2008