1o7f: Difference between revisions

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<StructureSection load='1o7f' size='340' side='right'caption='[[1o7f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1o7f' size='340' side='right'caption='[[1o7f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1o7f]] 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=1O7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7F FirstGlance]. <br>
<table><tr><td colspan='2'>[[1o7f]] 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=1O7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7F FirstGlance]. <br>
</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=1o7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7f OCA], [https://pdbe.org/1o7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7f RCSB], [https://www.ebi.ac.uk/pdbsum/1o7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7f ProSAT]</span></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]] 2.5&#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=1o7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7f OCA], [https://pdbe.org/1o7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7f RCSB], [https://www.ebi.ac.uk/pdbsum/1o7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7f ProSAT]</span></td></tr>
</table>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o7f ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o7f ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:12469113</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1o7f" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Bos, J L]]
[[Category: Bos JL]]
[[Category: Prakash, B]]
[[Category: De Rooij J]]
[[Category: Rehmann, H]]
[[Category: Prakash B]]
[[Category: Rooij, J De]]
[[Category: Rehmann H]]
[[Category: Rueppel, A]]
[[Category: Rueppel A]]
[[Category: Wittinghofer, A]]
[[Category: Wittinghofer A]]
[[Category: Wolf, E]]
[[Category: Wolf E]]
[[Category: Camp]]
[[Category: Camp-gef2]]
[[Category: Campb binding doamin]]
[[Category: Epac2]]
[[Category: Exchange factor]]
[[Category: Gef]]
[[Category: Regulation]]
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