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[[Image:1daw.jpg|left|200px]]
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{{STRUCTURE_1daw|  PDB=1daw  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-AMPPNP'''


==CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-AMPPNP==
<StructureSection load='1daw' size='340' side='right'caption='[[1daw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1daw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DAW 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1daw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1daw OCA], [https://pdbe.org/1daw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1daw RCSB], [https://www.ebi.ac.uk/pdbsum/1daw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1daw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CSK2A_MAIZE CSK2A_MAIZE] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site.
== 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/da/1daw_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=1daw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP were determined to 2.2 A resolution. Unlike most other protein kinases, CK2 from various sources shows 'dual-cosubstrate specificity', that is, the ability to efficiently use either ATP or GTP as a cosubstrate. The structures of these complexes demonstrate that water molecules are critical to switch the active site of CK2 from an ATP- to a GTP-compatible state. An understanding of the structural basis of dual-cosubstrate specificity may help in the design of drugs that target CK2 or other kinases with this property.


==Overview==
GTP plus water mimic ATP in the active site of protein kinase CK2.,Niefind K, Putter M, Guerra B, Issinger OG, Schomburg D Nat Struct Biol. 1999 Dec;6(12):1100-3. PMID:10581548<ref>PMID:10581548</ref>
The structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP were determined to 2.2 A resolution. Unlike most other protein kinases, CK2 from various sources shows 'dual-cosubstrate specificity', that is, the ability to efficiently use either ATP or GTP as a cosubstrate. The structures of these complexes demonstrate that water molecules are critical to switch the active site of CK2 from an ATP- to a GTP-compatible state. An understanding of the structural basis of dual-cosubstrate specificity may help in the design of drugs that target CK2 or other kinases with this property.


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


==Reference==
==See Also==
GTP plus water mimic ATP in the active site of protein kinase CK2., Niefind K, Putter M, Guerra B, Issinger OG, Schomburg D, Nat Struct Biol. 1999 Dec;6(12):1100-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10581548 10581548]
*[[Casein kinase 3D structures|Casein kinase 3D structures]]
[[Category: Non-specific serine/threonine protein kinase]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Guerra, B.]]
[[Category: Guerra B]]
[[Category: Issinger, O G.]]
[[Category: Issinger OG]]
[[Category: Niefind, K.]]
[[Category: Niefind K]]
[[Category: Puetter, M.]]
[[Category: Puetter M]]
[[Category: Schomburg, D.]]
[[Category: Schomburg D]]
[[Category: Binary complex]]
[[Category: Dual-cosubstrate specificity]]
[[Category: Protein kinase ck2]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:38:35 2008''

Latest revision as of 05:56, 9 August 2023

CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-AMPPNP

1daw, resolution 2.20Å

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