1r2a

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(New page: 200px<br /><applet load="1r2a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2a" /> '''THE MOLECULAR BASIS FOR PROTEIN KINASE A ANC...)
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[[Image:1r2a.gif|left|200px]]<br /><applet load="1r2a" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1r2a" />
 
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'''THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR'''<br />
 
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==Overview==
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==THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR==
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Compartmentalization of signal transduction enzymes into signaling, complexes is an important mechanism to ensure the specificity of, intracellular events. Formation of these complexes is mediated by, specialized protein motifs that participate in protein-protein, interactions. The adenosine 3',5'-cyclic monophosphate (cAMP)-dependent, protein kinase (PKA) is localized through interaction of the regulatory, (R) subunit dimer with A-kinase-anchoring proteins (AKAPs). We now report, the solution structure of the type II PKA R-subunit fragment, RIIalpha(1-44), which encompasses both the AKAP-binding and dimerization, interfaces. This structure incorporates an X-type four-helix bundle, dimerization motif with an extended hydrophobic face that is necessary for, high-affinity AKAP binding. NMR data on the complex between RIIalpha(1-44), and an AKAP fragment reveals extensive contacts between the two proteins., Interestingly, this same dimerization motif is present in other signaling, molecules, the S100 family. Therefore, the X-type four-helix bundle may, represent a conserved fold for protein-protein interactions in signal, transduction.
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<StructureSection load='1r2a' size='340' side='right'caption='[[1r2a]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1r2a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R2A FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r2a OCA], [https://pdbe.org/1r2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r2a RCSB], [https://www.ebi.ac.uk/pdbsum/1r2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r2a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KAP2_MOUSE KAP2_MOUSE] Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r2/1r2a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1r2a ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Compartmentalization of signal transduction enzymes into signaling complexes is an important mechanism to ensure the specificity of intracellular events. Formation of these complexes is mediated by specialized protein motifs that participate in protein-protein interactions. The adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) is localized through interaction of the regulatory (R) subunit dimer with A-kinase-anchoring proteins (AKAPs). We now report the solution structure of the type II PKA R-subunit fragment RIIalpha(1-44), which encompasses both the AKAP-binding and dimerization interfaces. This structure incorporates an X-type four-helix bundle dimerization motif with an extended hydrophobic face that is necessary for high-affinity AKAP binding. NMR data on the complex between RIIalpha(1-44) and an AKAP fragment reveals extensive contacts between the two proteins. Interestingly, this same dimerization motif is present in other signaling molecules, the S100 family. Therefore, the X-type four-helix bundle may represent a conserved fold for protein-protein interactions in signal transduction.
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==About this Structure==
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The molecular basis for protein kinase A anchoring revealed by solution NMR.,Newlon MG, Roy M, Morikis D, Hausken ZE, Coghlan V, Scott JD, Jennings PA Nat Struct Biol. 1999 Mar;6(3):222-7. PMID:10074940<ref>PMID:10074940</ref>
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1R2A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R2A OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The molecular basis for protein kinase A anchoring revealed by solution NMR., Newlon MG, Roy M, Morikis D, Hausken ZE, Coghlan V, Scott JD, Jennings PA, Nat Struct Biol. 1999 Mar;6(3):222-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10074940 10074940]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1r2a" style="background-color:#fffaf0;"></div>
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Single protein]]
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[[Category: Coghlan, V.]]
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[[Category: Hausken, Z.E.]]
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[[Category: Jennings, P.A.]]
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[[Category: Morikis, D.]]
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[[Category: Newlon, M.G.]]
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[[Category: Roy, M.]]
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[[Category: Scott, J.D.]]
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[[Category: anchoring]]
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[[Category: four-helix bundle]]
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[[Category: regulatory subunit]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:13:09 2007''
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==See Also==
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*[[CAMP-dependent protein kinase 3D structures|CAMP-dependent protein kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Coghlan V]]
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[[Category: Hausken ZE]]
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[[Category: Jennings PA]]
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[[Category: Morikis D]]
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[[Category: Newlon MG]]
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[[Category: Roy M]]
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[[Category: Scott JD]]

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THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR

PDB ID 1r2a

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