2bhh

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[[Image:2bhh.gif|left|200px]]
 
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==HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE INHIBITOR 4-HYDROXYPIPERINDINESULFONYL-INDIRUBINE==
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The line below this paragraph, containing "STRUCTURE_2bhh", creates the "Structure Box" on the page.
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<StructureSection load='2bhh' size='340' side='right'caption='[[2bhh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bhh]] 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=2BHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHH FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RYU:(2E,3S)-3-HYDROXY-5-[(4-HYDROXYPIPERIDIN-1-YL)SULFONYL]-3-METHYL-1,3-DIHYDRO-2,3-BIINDOL-2(1H)-ONE'>RYU</scene></td></tr>
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{{STRUCTURE_2bhh| PDB=2bhh | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhh OCA], [https://pdbe.org/2bhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhh RCSB], [https://www.ebi.ac.uk/pdbsum/2bhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDK2_HUMAN CDK2_HUMAN] Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization.<ref>PMID:10499802</ref> <ref>PMID:11051553</ref> <ref>PMID:10995386</ref> <ref>PMID:10995387</ref> <ref>PMID:10884347</ref> <ref>PMID:11113184</ref> <ref>PMID:15800615</ref> <ref>PMID:18372919</ref> <ref>PMID:20147522</ref> <ref>PMID:20079829</ref> <ref>PMID:20935635</ref> <ref>PMID:20195506</ref> <ref>PMID:19966300</ref> <ref>PMID:21262353</ref> <ref>PMID:21596315</ref> <ref>PMID:21319273</ref> <ref>PMID:17495531</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bhh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2bhh ConSurf].
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<div style="clear:both"></div>
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'''HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE INHIBITOR 4-HYDROXYPIPERINDINESULFONYL-INDIRUBINE'''
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==See Also==
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*[[Cyclin-dependent kinase 3D structures|Cyclin-dependent kinase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2BHH 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=2BHH OCA].
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__TOC__
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</StructureSection>
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==Reference==
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From the insoluble dye indirubin towards highly active, soluble CDK2-inhibitors., Jautelat R, Brumby T, Schafer M, Briem H, Eisenbrand G, Schwahn S, Kruger M, Lucking U, Prien O, Siemeister G, Chembiochem. 2005 Mar;6(3):531-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15742375 15742375]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Briem H]]
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[[Category: Briem, H.]]
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[[Category: Brumby T]]
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[[Category: Brumby, T.]]
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[[Category: Eisenbrand G]]
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[[Category: Eisenbrand, G.]]
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[[Category: Jautelat R]]
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[[Category: Jautelat, R.]]
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[[Category: Krueger M]]
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[[Category: Krueger, M.]]
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[[Category: Luecking U]]
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[[Category: Luecking, U.]]
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[[Category: Prien O]]
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[[Category: Prien, O.]]
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[[Category: Schaefer M]]
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[[Category: Schaefer, M.]]
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[[Category: Schwahn S]]
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[[Category: Schwahn, S.]]
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[[Category: Siemeister G]]
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[[Category: Siemeister, G.]]
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[[Category: 3d-structure]]
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[[Category: Arylamine n-acetyltransferase]]
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[[Category: Atp-binding]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]
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[[Category: Drug metabolism]]
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[[Category: Isoniazid]]
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[[Category: Mitosis]]
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[[Category: Mycobacteria]]
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[[Category: Nat]]
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[[Category: Phosphorylation]]
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[[Category: Polymorphism]]
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[[Category: Serine-threonine-protein kinase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:17:43 2008''
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Current revision

HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE INHIBITOR 4-HYDROXYPIPERINDINESULFONYL-INDIRUBINE

PDB ID 2bhh

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