1f0q: Difference between revisions

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New page: left|200px<br /><applet load="1f0q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f0q, resolution 2.63Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1f0q.jpg|left|200px]]<br /><applet load="1f0q" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f0q, resolution 2.63&Aring;" />
'''CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN==
The structure of a complex between the catalytic subunit of Zea mays CK2, and the nucleotide binding site-directed inhibitor emodin, (3-methyl-1,6,8-trihydroxyanthraquinone) was solved at 2.6-A resolution., Emodin enters the nucleotide binding site of the enzyme, filling a, hydrophobic pocket between the N-terminal and the C-terminal lobes, in the, proximity of the site occupied by the base rings of the natural, co-substrates. The interactions between the inhibitor and CK2 alpha are, mainly hydrophobic. Although the C-terminal domain of the enzyme is, essentially identical to the ATP-bound form, the beta-sheet in the, N-terminal domain is altered by the presence of emodin. The structural, data presented here highlight the flexibility of the kinase domain, structure and provide information for the design of selective ATP, competitive inhibitors of protein kinase CK2.
<StructureSection load='1f0q' size='340' side='right'caption='[[1f0q]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f0q]] 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=1F0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F0Q 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]] 2.63&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EMO:3-METHYL-1,6,8-TRIHYDROXYANTHRAQUINONE'>EMO</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=1f0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0q OCA], [https://pdbe.org/1f0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f0q RCSB], [https://www.ebi.ac.uk/pdbsum/1f0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0q 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/f0/1f0q_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=1f0q ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with EMO as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1F0Q OCA].
*[[Casein kinase 3D structures|Casein kinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2., Battistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA, J Biol Chem. 2000 Sep 22;275(38):29618-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10882732 10882732]
[[Category: Large Structures]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Single protein]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Battistutta, R.]]
[[Category: Battistutta R]]
[[Category: Moliner, E.De.]]
[[Category: De Moliner E]]
[[Category: Papinutto, E.]]
[[Category: Papinutto E]]
[[Category: Pinna, L.A.]]
[[Category: Pinna LA]]
[[Category: Sarno, S.]]
[[Category: Sarno S]]
[[Category: Zanotti, G.]]
[[Category: Zanotti G]]
[[Category: EMO]]
[[Category: protein kinase-inhibitor complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:30:25 2007''

Latest revision as of 10:09, 7 February 2024

CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODINCRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN

Structural highlights

1f0q is a 1 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.63Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1f0q, resolution 2.63Å

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