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3im3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of PKA RI alpha dimerization/docking domain== | |
| + | <StructureSection load='3im3' size='340' side='right'caption='[[3im3]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3im3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IM3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3im4|3im4]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRKAR1A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=3im3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3im3 OCA], [https://pdbe.org/3im3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3im3 RCSB], [https://www.ebi.ac.uk/pdbsum/3im3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3im3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/KAP0_BOVIN KAP0_BOVIN]] Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. | ||
| + | == 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/im/3im3_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=3im3 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A-kinase anchoring proteins (AKAPs) regulate cyclic AMP-dependent protein kinase (PKA) signaling in space and time. Dual-specific AKAP 2 (D-AKAP2) binds to the dimerization/docking (D/D) domain of both RI and RII regulatory subunits of PKA with high affinity. Here we have determined the structures of the RIalpha D/D domain alone and in complex with D-AKAP2. The D/D domain presents an extensive surface for binding through a well-formed N-terminal helix, and this surface restricts the diversity of AKAPs that can interact. The structures also underscore the importance of a redox-sensitive disulfide in affecting AKAP binding. An unexpected shift in the helical register of D-AKAP2 compared to the RIIalpha:D-AKAP2 complex structure makes the mode of binding to RIalpha novel. Finally, the comparison allows us to deduce a molecular explanation for the sequence and spatial determinants of AKAP specificity. | ||
| - | + | Structure of D-AKAP2:PKA RI complex: insights into AKAP specificity and selectivity.,Sarma GN, Kinderman FS, Kim C, von Daake S, Chen L, Wang BC, Taylor SS Structure. 2010 Feb 10;18(2):155-66. PMID:20159461<ref>PMID:20159461</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3im3" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[CAMP-dependent protein kinase 3D structures|CAMP-dependent protein kinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bovin]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Daake, S von]] | ||
| + | [[Category: Kim, C]] | ||
| + | [[Category: Kinderman, F S]] | ||
| + | [[Category: Sarma, G N]] | ||
| + | [[Category: Taylor, S S]] | ||
| + | [[Category: Acetylation]] | ||
| + | [[Category: Camp]] | ||
| + | [[Category: Camp-binding]] | ||
| + | [[Category: Disulfide bond]] | ||
| + | [[Category: Helix-turn-helix]] | ||
| + | [[Category: Nucleotide-binding]] | ||
| + | [[Category: Phosphoprotein]] | ||
| + | [[Category: Signaling protein]] | ||
| + | [[Category: Structural protein]] | ||
Current revision
Crystal structure of PKA RI alpha dimerization/docking domain
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