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| | <StructureSection load='3cf6' size='340' side='right'caption='[[3cf6]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3cf6' size='340' side='right'caption='[[3cf6]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cf6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [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=3CF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CF6 FirstGlance]. <br> | + | <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='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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2byv|2byv]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rapgef4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), RAP1B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> | | <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> | | </table> |
| | == Function == | | == 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>
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Arias-Palomo, E]] | + | [[Category: Arias-Palomo E]] |
| - | [[Category: Bos, J L]] | + | [[Category: Bos JL]] |
| - | [[Category: Hadders, M A]] | + | [[Category: Hadders MA]] |
| - | [[Category: Llorca, O]] | + | [[Category: Llorca O]] |
| - | [[Category: Rehmann, H]] | + | [[Category: Rehmann H]] |
| - | [[Category: Schwede, F]] | + | [[Category: Schwede F]] |
| - | [[Category: Camp]]
| + | |
| - | [[Category: Epac]]
| + | |
| - | [[Category: G-protein]]
| + | |
| - | [[Category: Gef]]
| + | |
| - | [[Category: Gtp-binding]]
| + | |
| - | [[Category: Gunanine nucleotide exchange factor]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Rap]]
| + | |
| - | [[Category: Rap1b]]
| + | |
| - | [[Category: Rapgef4]]
| + | |
| - | [[Category: Signaling protein regulator-gtp-binding protein complex]]
| + | |
| - | [[Category: Signaling protein-gtp-binding protein complex]]
| + | |
| - | [[Category: Sp-camp]]
| + | |
| Structural highlights
Function
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.[1] [2]
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 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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lampugnani MG, Orsenigo F, Rudini N, Maddaluno L, Boulday G, Chapon F, Dejana E. CCM1 regulates vascular-lumen organization by inducing endothelial polarity. J Cell Sci. 2010 Apr 1;123(Pt 7):1073-80. doi: 10.1242/jcs.059329. PMID:20332120 doi:10.1242/jcs.059329
- ↑ Rehmann H, Arias-Palomo E, Hadders MA, Schwede F, Llorca O, Bos JL. Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B. Nature. 2008 Sep 4;455(7209):124-7. Epub 2008 Jul 27. PMID:18660803 doi:http://dx.doi.org/10.1038/nature07187
- ↑ Rehmann H, Arias-Palomo E, Hadders MA, Schwede F, Llorca O, Bos JL. Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B. Nature. 2008 Sep 4;455(7209):124-7. Epub 2008 Jul 27. PMID:18660803 doi:http://dx.doi.org/10.1038/nature07187
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