3cf6
From Proteopedia
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| - | {{STRUCTURE_3cf6| PDB=3cf6 | SCENE= }} | ||
| - | ===Structure of Epac2 in complex with cyclic-AMP and Rap=== | ||
| - | {{ABSTRACT_PUBMED_18660803}} | ||
| - | == | + | ==Structure of Epac2 in complex with cyclic-AMP and Rap== |
| - | [[http://www.uniprot.org/uniprot/RAP1B_HUMAN RAP1B_HUMAN | + | <StructureSection load='3cf6' size='340' side='right'caption='[[3cf6]], [[Resolution|resolution]] 2.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3cf6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CF6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SP1:6-(6-AMINO-PURIN-9-YL)-2-THIOXO-TETRAHYDRO-2-FURO[3,2-D][1,3,2]DIOXAPHOSPHININE-2,7-DIOL'>SP1</scene></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=3cf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cf6 OCA], [https://pdbe.org/3cf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cf6 RCSB], [https://www.ebi.ac.uk/pdbsum/3cf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cf6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RAP1B_HUMAN RAP1B_HUMAN] GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction.<ref>PMID:20332120</ref> <ref>PMID:18660803</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/3cf6_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3cf6 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Epac proteins are activated by binding of the second messenger cAMP and then act as guanine nucleotide exchange factors for Rap proteins. The Epac proteins are involved in the regulation of cell adhesion and insulin secretion. Here we have determined the structure of Epac2 in complex with a cAMP analogue (Sp-cAMPS) and RAP1B by X-ray crystallography and single particle electron microscopy. The structure represents the cAMP activated state of the Epac2 protein with the RAP1B protein trapped in the course of the exchange reaction. Comparison with the inactive conformation reveals that cAMP binding causes conformational changes that allow the cyclic nucleotide binding domain to swing from a position blocking the Rap binding site towards a docking site at the Ras exchange motif domain. | ||
| - | + | Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B.,Rehmann H, Arias-Palomo E, Hadders MA, Schwede F, Llorca O, Bos JL Nature. 2008 Sep 4;455(7209):124-7. Epub 2008 Jul 27. PMID:18660803<ref>PMID:18660803</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | <div class="pdbe-citations 3cf6" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Arias-Palomo | + | __TOC__ |
| - | [[Category: Bos | + | </StructureSection> |
| - | [[Category: Hadders | + | [[Category: Homo sapiens]] |
| - | [[Category: Llorca | + | [[Category: Large Structures]] |
| - | [[Category: Rehmann | + | [[Category: Mus musculus]] |
| - | [[Category: Schwede | + | [[Category: Arias-Palomo E]] |
| - | + | [[Category: Bos JL]] | |
| - | + | [[Category: Hadders MA]] | |
| - | + | [[Category: Llorca O]] | |
| - | + | [[Category: Rehmann H]] | |
| - | + | [[Category: Schwede F]] | |
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Current revision
Structure of Epac2 in complex with cyclic-AMP and Rap
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