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2byv

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Structure of the cAMP responsive exchange factor Epac2 in its auto- inhibited state

Structural highlights

2byv is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPGF4_MOUSE Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ozaki N, Shibasaki T, Kashima Y, Miki T, Takahashi K, Ueno H, Sunaga Y, Yano H, Matsuura Y, Iwanaga T, Takai Y, Seino S. cAMP-GEFII is a direct target of cAMP in regulated exocytosis. Nat Cell Biol. 2000 Nov;2(11):805-11. PMID:11056535 doi:http://dx.doi.org/10.1038/35041046
↑ Rehmann H, Das J, Knipscheer P, Wittinghofer A, Bos JL. Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state. Nature. 2006 Feb 2;439(7076):625-8. PMID:16452984 doi:10.1038/nature04468

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2byv"

Categories: Large Structures | Mus musculus | Bos JL | Rehmann H | Wittinghofer A

@@ Line 3: / Line 3: @@
 <StructureSection load='2byv' size='340' side='right'caption='[[2byv]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2byv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BYV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2byv]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BYV FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o7f|1o7f]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2byv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byv OCA], [https://pdbe.org/2byv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2byv RCSB], [https://www.ebi.ac.uk/pdbsum/2byv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2byv ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RPGF4_MOUSE RPGF4_MOUSE] Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2.<ref>PMID:11056535</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Bos, J L]]
+[[Category: Bos JL]]
-[[Category: Rehmann, H]]
+[[Category: Rehmann H]]
-[[Category: Wittinghofer, A]]
+[[Category: Wittinghofer A]]
-[[Category: Auto-inhibition]]
-[[Category: Camp]]
-[[Category: Camp-gef2]]
-[[Category: Cdc25 homology domain]]
-[[Category: Cyclic nucleotide]]
-[[Category: Epac2]]
-[[Category: Exchange factor]]
-[[Category: Gef]]
-[[Category: Regulation]]

2byv

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Current revision

Structure of the cAMP responsive exchange factor Epac2 in its auto- inhibited state

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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