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[[Image:2i53.jpg|left|200px]]


{{Structure
==Crystal structure of Cyclin K==
|PDB= 2i53 |SIZE=350|CAPTION= <scene name='initialview01'>2i53</scene>, resolution 1.50&Aring;
<StructureSection load='2i53' size='340' side='right'caption='[[2i53]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>
<table><tr><td colspan='2'>[[2i53]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I53 FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
|GENE= CCNK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i53 OCA], [https://pdbe.org/2i53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i53 RCSB], [https://www.ebi.ac.uk/pdbsum/2i53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i53 ProSAT]</span></td></tr>
|RELATEDENTRY=[[1jkw|1JKW]], [[1kxu|1KXU]], [[1vin|1VIN]], [[1bu2|1BU2]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i53 OCA], [http://www.ebi.ac.uk/pdbsum/2i53 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i53 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CCNK_HUMAN CCNK_HUMAN] May play a role in transcriptional regulation. In vitro, is associated with a kinase activity toward both RNA polymerase II C-terminal domain and CDK2 (CAK).<ref>PMID:10574912</ref>
== 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/i5/2i53_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=2i53 ConSurf].
<div style="clear:both"></div>


'''Crystal structure of Cyclin K'''
==See Also==
 
*[[Cyclin 3D structures|Cyclin 3D structures]]
 
== References ==
==Overview==
<references/>
Cyclin K and the closely related cyclins T1, T2a, and T2b interact with cyclin-dependent kinase 9 (CDK9) forming multiple nuclear complexes, referred to collectively as positive transcription elongation factor b (P-TEFb). Through phosphorylation of the C-terminal domain of the RNA polymerase II largest subunit, distinct P-TEFb species regulate the transcriptional elongation of specific genes that play central roles in human physiology and disease development, including cardiac hypertrophy and human immunodeficiency virus-1 pathogenesis. We have determined the crystal structure of human cyclin K (residues 11-267) at 1.5 A resolution, which represents the first atomic structure of a P-TEFb subunit. The cyclin K fold comprises two typical cyclin boxes with two short helices preceding the N-terminal box. A prominent feature of cyclin K is an additional helix (H4a) in the first cyclin box that obstructs the binding pocket for the cell-cycle inhibitor p27(Kip1). Modeling of CDK9 bound to cyclin K provides insights into the structural determinants underlying the formation and regulation of this complex. A homology model of human cyclin T1 generated using the cyclin K structure as a template reveals that the two proteins have similar structures, as expected from their high level of sequence identity. Nevertheless, their CDK9-interacting surfaces display significant structural differences, which could potentially be exploited for the design of cyclin-targeted inhibitors of the CDK9-cyclin K and CDK9-cyclin T1 complexes.
__TOC__
 
</StructureSection>
==About this Structure==
2I53 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I53 OCA].
 
==Reference==
Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9., Baek K, Brown RS, Birrane G, Ladias JA, J Mol Biol. 2007 Feb 16;366(2):563-73. Epub 2006 Nov 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17169370 17169370]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Baek, K.]]
[[Category: Baek K]]
[[Category: Birrane, G.]]
[[Category: Birrane G]]
[[Category: Brown, R S.]]
[[Category: Brown RS]]
[[Category: Ladias, J A.A.]]
[[Category: Ladias JAA]]
[[Category: cdk9]]
[[Category: cell cycle]]
[[Category: cyclin box]]
[[Category: cyclin k]]
[[Category: p-tefb]]
[[Category: positive transcription elongation factor]]
[[Category: transcription]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:39:53 2008''

Latest revision as of 09:01, 21 February 2024

Crystal structure of Cyclin K

2i53, resolution 1.50Å

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