2ezw: Difference between revisions

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[[Image:2ezw.png|left|200px]]


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==Solution structure of the docking and dimerization domain of the type I alpha regulatory subunit of protein kinase A (RIalpha D/D)==
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<StructureSection load='2ezw' size='340' side='right'caption='[[2ezw]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2ezw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EZW FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r2a|1r2a]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRKAR1A (amino acids:12 - 61) ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
{{STRUCTURE_2ezw|  PDB=2ezw  |  SCENE=  }}
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transferase Transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </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=2ezw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezw OCA], [https://pdbe.org/2ezw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ezw RCSB], [https://www.ebi.ac.uk/pdbsum/2ezw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ezw 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/ez/2ezw_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=2ezw ConSurf].
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== Publication Abstract from PubMed ==
The subcellular localization of cAMP-dependent protein kinase (PKA) occurs through interaction with A-Kinase Anchoring Proteins (AKAPs). AKAPs bind to the PKA regulatory subunit dimer of both type Ialpha and type IIalpha (RIalpha and RIIalpha). RIalpha and RIIalpha display characteristic localization within different cell types, which is maintained by interaction of AKAPs with the N-terminal dimerization and docking domain (D/D) of the respective regulatory subunit. Previously, we reported the solution structure of RIIa D/D module, both free and bound to AKAPs. We have now solved the solution structure of the dimerization and docking domain of the type Ialpha regulatory dimer subunit (RIalpha D/D). RIalpha D/D is a compact docking module, with unusual interchain disulfide bonds that help maintain the AKAP interaction surface. In contrast to the shallow hydrophobic groove for AKAP binding across the surface of the RIIalpha D/D dimeric interface, the RIalpha D/D module presents a deep cleft for proposed AKAP binding. RIalpha and RIIalpha D/D interaction modules present drastically differing dimeric topographies, despite a conserved X-type four-helix bundle structure.


===Solution structure of the docking and dimerization domain of the type I alpha regulatory subunit of protein kinase A (RIalpha D/D)===
Related protein-protein interaction modules present drastically different surface topographies despite a conserved helical platform.,Banky P, Roy M, Newlon MG, Morikis D, Haste NM, Taylor SS, Jennings PA J Mol Biol. 2003 Jul 25;330(5):1117-29. PMID:12860132<ref>PMID:12860132</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2ezw" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12860132}}, adds the Publication Abstract to the page
*[[CAMP-dependent protein kinase 3D structures|CAMP-dependent protein kinase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12860132 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12860132}}
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</StructureSection>
==About this Structure==
[[Category: Bovin]]
2EZW is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZW OCA].
[[Category: Large Structures]]
 
[[Category: Transferase]]
==Reference==
[[Category: Banky, P]]
<ref group="xtra">PMID:12860132</ref><references group="xtra"/>
[[Category: Bos taurus]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Banky, P.]]
[[Category: Anchoring]]
[[Category: Anchoring]]
[[Category: Four-helix bundle]]
[[Category: Four-helix bundle]]
[[Category: Regulatory subunit]]
[[Category: Regulatory subunit]]
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