3unk - Revision history

OCA at 14:03, 14 March 2024

2024-03-14T14:03:09Z

← Older revision		Revision as of 14:03, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3unk' size='340' side='right'caption='[[3unk]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3unk' size='340' side='right'caption='[[3unk]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3unk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNK FirstGlance]. <br>		<table><tr><td colspan='2'>[[3unk]] 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=3UNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNK FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=0BY:4-({4~~-[~~(2-CHLOROPHENYL)AMINO~~]~~PYRIMIDIN-~~2~~-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.1Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'~~>~~[[3unj\|3unj]], [[3unz\|3unz]], [[3uo4\|3uo4]], [[3uo5\|3uo5]], [[3uo6\|3uo6]], [[3uod\|3uod]], [[3uoh\|3uoh]], [[3uoj\|3uoj]], [[3uok\|3uok]], [[3uol\|3uol]], [[3up2\|3up2]], [[3up7\|3up7]]~~<~~/div></td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0BY:4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">CDK2~~ ([~~https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN~~])~~</td~~></tr>
	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22]~~ </~~span~~></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=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [https://pdbe.org/3unk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [https://www.ebi.ac.uk/pdbsum/3unk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unk ProSAT]</span></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=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [https://pdbe.org/3unk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [https://www.ebi.ac.uk/pdbsum/3unk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[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>		[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>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Most protein kinases share a DFG (Asp-Phe-Gly) motif in the ATP site which can assume two distinct conformations, the active DFG-in and the inactive DFG-out states. Small molecule inhibitors able to induce the DFG-out state have received considerable attention in kinase drug discovery. Using a typical DFG-in inhibitor scaffold of Aurora A, a kinase involved in the regulation of cell division, we found that halogen and nitrile substituents directed at the N-terminally flanking residue Ala273 induced global conformational changes in the enzyme, leading to DFG-out inhibitors that are among the most potent Aurora A inhibitors reported to date. The data suggest an unprecedented mechanism of action, in which induced-dipole forces along the Ala273 side chain alter the charge distribution of the DFG backbone, allowing the DFG to unwind. As the ADFG sequence and three-dimensional structure is highly conserved, DFG-out inhibitors of other kinases may be designed by specifically targeting the flanking alanine residue with electric dipoles.

	A novel mechanism by which small molecule inhibitors induce the DFG flip in Aurora A.,Martin MP, Zhu JY, Lawrence H, Pireddu R, Luo Y, Alam R, Ozcan S, Sebti SM, Lawrence NJ, Schonbrunn E ACS Chem Biol. 2012 Jan 16. PMID:22248356<ref>PMID:22248356</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3unk" style="background-color:#fffaf0;"></div~~>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Cyclin-dependent kinase]]~~		[[Category: Homo sapiens]]
	~~[[Category: Human~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Alam, R]]		[[Category: Alam R]]
	[[Category: Martin~~, M P~~]]		[[Category: Martin MP]]
	[[Category: Schonbrunn, E]]		[[Category: Schonbrunn E]]
	[[Category: Zhu, J Y]]		[[Category: Zhu J-Y]]
	~~[[Category: Allosteric ligand]]~~
	~~[[Category: Some]]~~
	~~[[Category: Protein kinase]]~~
	~~[[Category: Transferase-transferase inhibitor complex~~]]

OCA at 07:50, 20 July 2022

2022-07-20T07:50:58Z

← Older revision		Revision as of 07:50, 20 July 2022
Line 1:		Line 1:

	==CDK2 in complex with inhibitor YL5-083==		==CDK2 in complex with inhibitor YL5-083==
	<StructureSection load='3unk' size='340' side='right' caption='[[3unk]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3unk' size='340' side='right'caption='[[3unk]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3unk]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3UNK FirstGlance]. <br>		<table><tr><td colspan='2'>[[3unk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0BY:4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0BY:4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3unj\|3unj]], [[3unz\|3unz]], [[3uo4\|3uo4]], [[3uo5\|3uo5]], [[3uo6\|3uo6]], [[3uod\|3uod]], [[3uoh\|3uoh]], [[3uoj\|3uoj]], [[3uok\|3uok]], [[3uol\|3uol]], [[3up2\|3up2]], [[3up7\|3up7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3unj\|3unj]], [[3unz\|3unz]], [[3uo4\|3uo4]], [[3uo5\|3uo5]], [[3uo6\|3uo6]], [[3uod\|3uod]], [[3uoh\|3uoh]], [[3uoj\|3uoj]], [[3uok\|3uok]], [[3uol\|3uol]], [[3up2\|3up2]], [[3up7\|3up7]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDK2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDK2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [~~http~~://pdbe.org/3unk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3unk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3unk ProSAT]</span></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=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [https://pdbe.org/3unk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [https://www.ebi.ac.uk/pdbsum/3unk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://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>		[[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
	*[[Cyclin-dependent kinase\|Cyclin-dependent kinase]]		*[[Cyclin-dependent kinase 3D structures\|Cyclin-dependent kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 30:
	[[Category: Cyclin-dependent kinase]]		[[Category: Cyclin-dependent kinase]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Alam, R]]		[[Category: Alam, R]]
	[[Category: Martin, M P]]		[[Category: Martin, M P]]
Line 35:		Line 36:
	[[Category: Zhu, J Y]]		[[Category: Zhu, J Y]]
	[[Category: Allosteric ligand]]		[[Category: Allosteric ligand]]
	[[Category: An]]		[[Category: Some]]
	[[Category: Protein kinase]]		[[Category: Protein kinase]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 16:13, 4 August 2016

2016-08-04T16:13:44Z

← Older revision		Revision as of 16:13, 4 August 2016
Line 1:		Line 1:

	==CDK2 in complex with inhibitor YL5-083==		==CDK2 in complex with inhibitor YL5-083==
	<StructureSection load='3unk' size='340' side='right' caption='[[3unk]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3unk' size='340' side='right' caption='[[3unk]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3unk]] is a 1 chain structure with 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=3UNK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UNK FirstGlance]. <br>		<table><tr><td colspan='2'>[[3unk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UNK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0BY:4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0BY:4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3unj\|3unj]], [[3unz\|3unz]], [[3uo4\|3uo4]], [[3uo5\|3uo5]], [[3uo6\|3uo6]], [[3uod\|3uod]], [[3uoh\|3uoh]], [[3uoj\|3uoj]], [[3uok\|3uok]], [[3uol\|3uol]], [[3up2\|3up2]], [[3up7\|3up7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3unj\|3unj]], [[3unz\|3unz]], [[3uo4\|3uo4]], [[3uo5\|3uo5]], [[3uo6\|3uo6]], [[3uod\|3uod]], [[3uoh\|3uoh]], [[3uoj\|3uoj]], [[3uok\|3uok]], [[3uol\|3uol]], [[3up2\|3up2]], [[3up7\|3up7]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [http://www.ebi.ac.uk/pdbsum/3unk PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [http://pdbe.org/3unk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [http://www.ebi.ac.uk/pdbsum/3unk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3unk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 3unk" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[~~Cell division protein~~ kinase 2\|~~Cell division protein~~ kinase 2]]		*[[Cyclin-dependent kinase\|Cyclin-dependent kinase]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Cyclin-dependent kinase]]		[[Category: Cyclin-dependent kinase]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Alam, R]]		[[Category: Alam, R]]
	[[Category: Martin, M P]]		[[Category: Martin, M P]]

OCA at 16:53, 24 December 2014

2014-12-24T16:53:56Z

← Older revision		Revision as of 16:53, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3unk]] is a 1 chain structure with 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=3UNK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UNK FirstGlance]. <br>		<table><tr><td colspan='2'>[[3unk]] is a 1 chain structure with 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=3UNK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UNK FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0BY:4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0BY:4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3unj\|3unj]], [[3unz\|3unz]], [[3uo4\|3uo4]], [[3uo5\|3uo5]], [[3uo6\|3uo6]], [[3uod\|3uod]], [[3uoh\|3uoh]], [[3uoj\|3uoj]], [[3uok\|3uok]], [[3uol\|3uol]], [[3up2\|3up2]], [[3up7\|3up7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3unj\|3unj]], [[3unz\|3unz]], [[3uo4\|3uo4]], [[3uo5\|3uo5]], [[3uo6\|3uo6]], [[3uod\|3uod]], [[3uoh\|3uoh]], [[3uoj\|3uoj]], [[3uok\|3uok]], [[3uol\|3uol]], [[3up2\|3up2]], [[3up7\|3up7]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [http://www.ebi.ac.uk/pdbsum/3unk PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [http://www.ebi.ac.uk/pdbsum/3unk PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 15:		Line 17:
	A novel mechanism by which small molecule inhibitors induce the DFG flip in Aurora A.,Martin MP, Zhu JY, Lawrence H, Pireddu R, Luo Y, Alam R, Ozcan S, Sebti SM, Lawrence NJ, Schonbrunn E ACS Chem Biol. 2012 Jan 16. PMID:22248356<ref>PMID:22248356</ref>		A novel mechanism by which small molecule inhibitors induce the DFG flip in Aurora A.,Martin MP, Zhu JY, Lawrence H, Pireddu R, Luo Y, Alam R, Ozcan S, Sebti SM, Lawrence NJ, Schonbrunn E ACS Chem Biol. 2012 Jan 16. PMID:22248356<ref>PMID:22248356</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>

	==See Also==		==See Also==
	*[[Cell division protein kinase\|Cell division protein kinase]]		*[[Cell division protein kinase 2\|Cell division protein kinase 2]]
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 28:
	[[Category: Cyclin-dependent kinase]]		[[Category: Cyclin-dependent kinase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Alam, R.]]		[[Category: Alam, R]]
	[[Category: Martin, M P.]]		[[Category: Martin, M P]]
	[[Category: Schonbrunn, E.]]		[[Category: Schonbrunn, E]]
	[[Category: Zhu, J Y.]]		[[Category: Zhu, J Y]]
	[[Category: Allosteric ligand]]		[[Category: Allosteric ligand]]
	[[Category: An]]		[[Category: An]]
	[[Category: Protein kinase]]		[[Category: Protein kinase]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 06:19, 5 June 2014

2014-06-05T06:19:56Z

← Older revision		Revision as of 06:19, 5 June 2014
Line 1:		Line 1:
	[[~~Image~~:~~3unk~~.~~png~~\|~~left~~\|~~200px~~]]		==CDK2 in complex with inhibitor YL5-083==
			<StructureSection load='3unk' size='340' side='right' caption='[[3unk]], [[Resolution\|resolution]] 2.10Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3unk]] is a 1 chain structure with 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=3UNK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UNK FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0BY:4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)BENZOIC+ACID'>0BY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3unj\|3unj]], [[3unz\|3unz]], [[3uo4\|3uo4]], [[3uo5\|3uo5]], [[3uo6\|3uo6]], [[3uod\|3uod]], [[3uoh\|3uoh]], [[3uoj\|3uoj]], [[3uok\|3uok]], [[3uol\|3uol]], [[3up2\|3up2]], [[3up7\|3up7]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclin-dependent_kinase Cyclin-dependent kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.22 2.7.11.22] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3unk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3unk RCSB], [http://www.ebi.ac.uk/pdbsum/3unk PDBsum]</span></td></tr>
			<table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Most protein kinases share a DFG (Asp-Phe-Gly) motif in the ATP site which can assume two distinct conformations, the active DFG-in and the inactive DFG-out states. Small molecule inhibitors able to induce the DFG-out state have received considerable attention in kinase drug discovery. Using a typical DFG-in inhibitor scaffold of Aurora A, a kinase involved in the regulation of cell division, we found that halogen and nitrile substituents directed at the N-terminally flanking residue Ala273 induced global conformational changes in the enzyme, leading to DFG-out inhibitors that are among the most potent Aurora A inhibitors reported to date. The data suggest an unprecedented mechanism of action, in which induced-dipole forces along the Ala273 side chain alter the charge distribution of the DFG backbone, allowing the DFG to unwind. As the ADFG sequence and three-dimensional structure is highly conserved, DFG-out inhibitors of other kinases may be designed by specifically targeting the flanking alanine residue with electric dipoles.

	~~<!--~~		A novel mechanism by which small molecule inhibitors induce the DFG flip in Aurora A.,Martin MP, Zhu JY, Lawrence H, Pireddu R, Luo Y, Alam R, Ozcan S, Sebti SM, Lawrence NJ, Schonbrunn E ACS Chem Biol. 2012 Jan 16. PMID:22248356<ref>PMID:22248356</ref>
	~~The line below this paragraph~~, ~~containing "STRUCTURE_3unk"~~, ~~creates the "Structure Box" on the page~~.
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display~~.
	-->
	~~{{STRUCTURE_3unk\| PDB=3unk \| SCENE= }}~~

	~~===CDK2 in complex with inhibitor YL5-083===~~		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
			</div>

			==See Also==
	~~<!--~~		*[[Cell division protein kinase\|Cell division protein kinase]]
	~~The line below this paragraph, {{ABSTRACT_PUBMED_22248356}}, adds the Publication Abstract to the page~~		== References ==
	~~(as it appears on PubMed at http://www.pubmed.gov), where 22248356 is the PubMed ID number.~~		<references/>
	~~-->~~		__TOC__
	~~{{ABSTRACT_PUBMED_22248356}}~~		</StructureSection>

	==~~About this Structure~~==
	[[~~3unk]~~] ~~is a 1 chain structure with 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=3UNK OCA].~~

	==~~Reference~~==
	<~~ref group="xtra">PMID:022248356<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Cyclin-dependent kinase]]		[[Category: Cyclin-dependent kinase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 07:30, 1 February 2012

2012-02-01T07:30:16Z

← Older revision		Revision as of 07:30, 1 February 2012
Line 1:		Line 1:
	[[Image:3unk.~~jpg~~\|left\|200px]]		[[Image:3unk.png\|left\|200px]]

	<!--		<!--

OCA at 06:28, 25 January 2012

2012-01-25T06:28:23Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:3unk.jpg|left|200px]]
-The entry 3unk is ON HOLD  until Paper Publication
+<!--
-Authors: Zhu, J.-Y., Martin, M.P., Alam, R., Schonbrunn, E.
+===CDK2 in complex with inhibitor YL5-083===
-Description: CDK2 in complex with inhibitor YL5-083

OCA at 11:10, 14 December 2011

2011-12-14T11:10:42Z

← Older revision		Revision as of 11:10, 14 December 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 3unk is ON HOLD		The entry 3unk is ON HOLD until Paper Publication

	Authors: Zhu, J.-Y., Martin, M.P., Alam, R., Schonbrunn, E.		Authors: Zhu, J.-Y., Martin, M.P., Alam, R., Schonbrunn, E.

	Description: CDK2 in complex with inhibitor YL5-083		Description: CDK2 in complex with inhibitor YL5-083

OCA at 07:36, 7 December 2011

2011-12-07T07:36:21Z

← Older revision		Revision as of 07:36, 7 December 2011
Line 5:		Line 5:
	Authors: Zhu, J.-Y., Martin, M.P., Alam, R., Schonbrunn, E.		Authors: Zhu, J.-Y., Martin, M.P., Alam, R., Schonbrunn, E.

	Description: CDK2 ~~IN COMPLEX WITH INHIBITOR~~ YL5-083		Description: CDK2 in complex with inhibitor YL5-083

OCA: Protected "3unk" [edit=sysop:move=sysop]

2011-11-23T18:40:34Z

Protected "3unk" [edit=sysop:move=sysop]

← Older revision	Revision as of 18:40, 23 November 2011
(No difference)