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New page: left|200px<br /><applet load="2hwn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hwn, resolution 1.600Å" /> '''Crystal Structure o...
 
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[[Image:2hwn.gif|left|200px]]<br /><applet load="2hwn" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2hwn, resolution 1.600&Aring;" />
'''Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide'''<br />


==Overview==
==Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide==
A kinase-anchoring proteins (AKAPs) target PKA to specific microdomains by, using an amphipathic helix that docks to N-terminal dimerization and, docking (D/D) domains of PKA regulatory (R) subunits. To understand, specificity, we solved the crystal structure of the helical motif from, D-AKAP2, a dual-specific AKAP, bound to the RIIalpha D/D domain. The 1.6, Angstrom structure reveals how this dynamic, hydrophobic docking site is, assembled. A stable, hydrophobic docking groove is formed by the helical, interface of two RIIalpha protomers. The flexible N terminus of one, protomer is then recruited to the site, anchored to the peptide through, two essential isoleucines. The other N terminus is disordered. This, asymmetry provides greater possibilities for AKAP docking. Although there, is strong discrimination against RIalpha in the N terminus of the AKAP, helix, the hydrophobic groove discriminates against RIIalpha. RIalpha, with a cavity in the groove, can accept a bulky tryptophan, whereas, RIIalpha requires valine.
<StructureSection load='2hwn' size='340' side='right'caption='[[2hwn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hwn]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Macaca_fascicularis Macaca fascicularis] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HWN 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2hwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hwn OCA], [https://pdbe.org/2hwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hwn RCSB], [https://www.ebi.ac.uk/pdbsum/2hwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hwn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KAP2_RAT KAP2_RAT] 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.
== 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/hw/2hwn_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=2hwn ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2HWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HWN OCA].
*[[CAMP-dependent protein kinase 3D structures|CAMP-dependent protein kinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
A dynamic mechanism for AKAP binding to RII isoforms of cAMP-dependent protein kinase., Kinderman FS, Kim C, von Daake S, Ma Y, Pham BQ, Spraggon G, Xuong NH, Jennings PA, Taylor SS, Mol Cell. 2006 Nov 3;24(3):397-408. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17081990 17081990]
[[Category: Large Structures]]
[[Category: Macaca fascicularis]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Kim C]]
[[Category: cAMP-dependent protein kinase]]
[[Category: Kinderman F]]
[[Category: Kim, C.]]
[[Category: Kinderman, F.]]
[[Category: GOL]]
[[Category: akap]]
[[Category: d/d]]
[[Category: dimerization/docking]]
[[Category: pka]]
[[Category: regulatory subunit]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:01:35 2007''

Latest revision as of 09:34, 14 February 2024

Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide

2hwn, resolution 1.60Å

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