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[[Image:1rqf.gif|left|200px]]
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{{STRUCTURE_1rqf|  PDB=1rqf  |  SCENE=  }}
'''Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide'''


==Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide==
<StructureSection load='1rqf' size='340' side='right'caption='[[1rqf]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rqf]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQF 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]] 2.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1rqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqf OCA], [https://pdbe.org/1rqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqf RCSB], [https://www.ebi.ac.uk/pdbsum/1rqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CSK2B_XENLA CSK2B_XENLA] Participates in Wnt signaling. Plays a complex role in regulating the basal catalytic activity of the alpha subunit (By similarity).
== 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/rq/1rqf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1rqf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A truncated form of the regulatory subunit of the protein kinase CK2beta (residues 1-178) has been crystallized in the presence of a fragment of the cyclin-dependent kinase inhibitor p21WAF1 (residues 46-65) and the structure solved at 2.9 A resolution by molecular replacement. The core of the CK2beta dimer shows a high structural similarity with that identified in previous structural analyses of the dimer and the holoenzyme. However, the electron density corresponding to the substrate-binding acidic loop (residues 55-64) indicates two conformations that differ from that of the holoenzyme structure [Niefind et al. (2001), EMBO J. 20, 5320-5331]. Difference electron density near the dimerization region in each of the eight protomers in the asymmetric unit is attributed to between one and eight amino-acid residues of a complexed fragment of p21WAF1. This binding site corresponds to the solvent-accessible part of the conserved zinc-finger motif.


==Overview==
Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop.,Bertrand L, Sayed MF, Pei XY, Parisini E, Dhanaraj V, Bolanos-Garcia VM, Allende JE, Blundell TL Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1698-704. Epub, 2004 Sep 23. PMID:15388915<ref>PMID:15388915</ref>
A truncated form of the regulatory subunit of the protein kinase CK2beta (residues 1-178) has been crystallized in the presence of a fragment of the cyclin-dependent kinase inhibitor p21WAF1 (residues 46-65) and the structure solved at 2.9 A resolution by molecular replacement. The core of the CK2beta dimer shows a high structural similarity with that identified in previous structural analyses of the dimer and the holoenzyme. However, the electron density corresponding to the substrate-binding acidic loop (residues 55-64) indicates two conformations that differ from that of the holoenzyme structure [Niefind et al. (2001), EMBO J. 20, 5320-5331]. Difference electron density near the dimerization region in each of the eight protomers in the asymmetric unit is attributed to between one and eight amino-acid residues of a complexed fragment of p21WAF1. This binding site corresponds to the solvent-accessible part of the conserved zinc-finger motif.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1RQF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQF OCA].
</div>
<div class="pdbe-citations 1rqf" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop., Bertrand L, Sayed MF, Pei XY, Parisini E, Dhanaraj V, Bolanos-Garcia VM, Allende JE, Blundell TL, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1698-704. Epub, 2004 Sep 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15388915 15388915]
*[[Casein kinase 3D structures|Casein kinase 3D structures]]
[[Category: Non-specific serine/threonine protein kinase]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Allende, J E.]]
[[Category: Allende JE]]
[[Category: Bertrand, L.]]
[[Category: Bertrand L]]
[[Category: Blundell, T L.]]
[[Category: Blundell TL]]
[[Category: Bolanos-Garcia, V M.]]
[[Category: Bolanos-Garcia VM]]
[[Category: Dhanaraj, V.]]
[[Category: Dhanaraj V]]
[[Category: Parisini, E.]]
[[Category: Parisini E]]
[[Category: Pei, X Y.]]
[[Category: Pei X-Y]]
[[Category: Sayed, M F.]]
[[Category: Sayed MF]]
[[Category: Casein kinase beta subunit]]
[[Category: Cyclin-dependent kinase inhibitor]]
[[Category: Ser/thr protein kinase]]
[[Category: Zn finger]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:47:28 2008''

Latest revision as of 06:30, 12 February 2025

Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide

1rqf, resolution 2.89Å

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