2cjm - Revision history

OCA at 14:19, 13 December 2023

2023-12-13T14:19:13Z

←Older revision		Revision as of 14:19, 13 December 2023
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	<StructureSection load='2cjm' size='340' side='right'caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2cjm' size='340' side='right'caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2CJM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CJM FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ATP:ADENOSINE~~-~~5-TRIPHOSPHATE'>ATP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.3Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~PTR~~:O-~~PHOSPHOTYROSINE~~'>~~PTR~~</scene>, <scene name='pdbligand=~~TPO~~:~~PHOSPHOTHREONINE~~'>~~TPO~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;~~'>[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1okv\|1okv]], [[1okw\|1okw]], [[1ol1\|1ol1]], [[1ol2\|1ol2]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pf8\|1pf8]], [[1pkd\|1pkd]], [[1pw2\|1pw2]], [[1pxi\|1pxi]], [[1pxj\|1pxj]], [[1pxk\|1pxk]], [[1pxl\|1pxl]], [[1pxm\|1pxm]], [[1pxn\|1pxn]], [[1pxo\|1pxo]], [[1pxp\|1pxp]], [[1pye\|1pye]], [[1qmz\|1qmz]], [[1r78\|1r78]], [[1urc\|1urc]], [[1urw\|1urw]], [[1v1k\|1v1k]], [[1vyw\|1vyw]], [[1vyz\|1vyz]], [[1w0x\|1w0x]], [[1w8c\|1w8c]], [[1w98\|1w98]], [[1wcc\|1wcc]], [[1y8y\|1y8y]], [[1y91\|1y91]], [[1ykr\|1ykr]], [[2a0c\|2a0c]], [[2b52\|2b52]], [[2b53\|2b53]], [[2b54\|2b54]], [[2b55\|2b55]], [[2bhe\|2bhe]], [[2bhh\|2bhh]], [[2bkz\|2bkz]], [[2bpm\|2bpm]], [[2btr\|2btr]], [[2bts\|2bts]], [[2c4g\|2c4g]], [[2c5n\|2c5n]], [[2c5o\|2c5o]], [[2c5p\|2c5p]], [[2c5t\|2c5t]], [[2c5v\|2c5v]], [[2c5x\|2c5x]], [[2c5y\|2c5y]], [[2c68\|2c68]], [[2c69\|2c69]], [[2c6i\|2c6i]], [[2c6k\|2c6k]], [[2c6l\|2c6l]], [[2c6m\|2c6m]], [[2c6o\|2c6o]], [[2c6t\|2c6t]], [[2cch\|2cch]], [[2cci\|2cci]], [[2exm\|2exm]]</~~div~~><~~/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=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [https://pdbe.org/2cjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [https://www.ebi.ac.uk/pdbsum/2cjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjm ProSAT]</span></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </~~span~~></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [~~http~~://pdbe.org/2cjm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2cjm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjm 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> ~~[[http://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN]] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.~~	+	[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Transferase]]~~	+	[[Category: Endicott JA]]
-	[[Category: Endicott~~, J A~~]]	+	[[Category: Johnson T]]
-	[[Category: Johnson, T]]	+	[[Category: Lindert L]]
-	[[Category: Lindert, L]]	+	[[Category: Morgan M]]
-	[[Category: Morgan, M]]	+	[[Category: Noble MEM]]
-	[[Category: Noble~~, M E.M~~]]	+	[[Category: Tucker J]]
-	[[Category: Tucker, J]]	+	[[Category: Welburn JPI]]
-	[[Category: Welburn~~, J P.I~~]]	+	[[Category: Willis A]]
-	[[Category: Willis, A]]	+
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Cell division]]~~	+
-	~~[[Category: Cyclin-dependent kinase]]~~	+
-	~~[[Category: Mitosis]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Regulation]]~~	+
-	~~[[Category: Serine/threonine-protein kinase~~]]	+

OCA at 04:55, 19 November 2020

2020-11-19T04:55:57Z

←Older revision		Revision as of 04:55, 19 November 2020
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	<StructureSection load='2cjm' size='340' side='right'caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2cjm' size='340' side='right'caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2CJM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2CJM FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1okv\|1okv]], [[1okw\|1okw]], [[1ol1\|1ol1]], [[1ol2\|1ol2]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pf8\|1pf8]], [[1pkd\|1pkd]], [[1pw2\|1pw2]], [[1pxi\|1pxi]], [[1pxj\|1pxj]], [[1pxk\|1pxk]], [[1pxl\|1pxl]], [[1pxm\|1pxm]], [[1pxn\|1pxn]], [[1pxo\|1pxo]], [[1pxp\|1pxp]], [[1pye\|1pye]], [[1qmz\|1qmz]], [[1r78\|1r78]], [[1urc\|1urc]], [[1urw\|1urw]], [[1v1k\|1v1k]], [[1vyw\|1vyw]], [[1vyz\|1vyz]], [[1w0x\|1w0x]], [[1w8c\|1w8c]], [[1w98\|1w98]], [[1wcc\|1wcc]], [[1y8y\|1y8y]], [[1y91\|1y91]], [[1ykr\|1ykr]], [[2a0c\|2a0c]], [[2b52\|2b52]], [[2b53\|2b53]], [[2b54\|2b54]], [[2b55\|2b55]], [[2bhe\|2bhe]], [[2bhh\|2bhh]], [[2bkz\|2bkz]], [[2bpm\|2bpm]], [[2btr\|2btr]], [[2bts\|2bts]], [[2c4g\|2c4g]], [[2c5n\|2c5n]], [[2c5o\|2c5o]], [[2c5p\|2c5p]], [[2c5t\|2c5t]], [[2c5v\|2c5v]], [[2c5x\|2c5x]], [[2c5y\|2c5y]], [[2c68\|2c68]], [[2c69\|2c69]], [[2c6i\|2c6i]], [[2c6k\|2c6k]], [[2c6l\|2c6l]], [[2c6m\|2c6m]], [[2c6o\|2c6o]], [[2c6t\|2c6t]], [[2cch\|2cch]], [[2cci\|2cci]], [[2exm\|2exm]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1okv\|1okv]], [[1okw\|1okw]], [[1ol1\|1ol1]], [[1ol2\|1ol2]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pf8\|1pf8]], [[1pkd\|1pkd]], [[1pw2\|1pw2]], [[1pxi\|1pxi]], [[1pxj\|1pxj]], [[1pxk\|1pxk]], [[1pxl\|1pxl]], [[1pxm\|1pxm]], [[1pxn\|1pxn]], [[1pxo\|1pxo]], [[1pxp\|1pxp]], [[1pye\|1pye]], [[1qmz\|1qmz]], [[1r78\|1r78]], [[1urc\|1urc]], [[1urw\|1urw]], [[1v1k\|1v1k]], [[1vyw\|1vyw]], [[1vyz\|1vyz]], [[1w0x\|1w0x]], [[1w8c\|1w8c]], [[1w98\|1w98]], [[1wcc\|1wcc]], [[1y8y\|1y8y]], [[1y91\|1y91]], [[1ykr\|1ykr]], [[2a0c\|2a0c]], [[2b52\|2b52]], [[2b53\|2b53]], [[2b54\|2b54]], [[2b55\|2b55]], [[2bhe\|2bhe]], [[2bhh\|2bhh]], [[2bkz\|2bkz]], [[2bpm\|2bpm]], [[2btr\|2btr]], [[2bts\|2bts]], [[2c4g\|2c4g]], [[2c5n\|2c5n]], [[2c5o\|2c5o]], [[2c5p\|2c5p]], [[2c5t\|2c5t]], [[2c5v\|2c5v]], [[2c5x\|2c5x]], [[2c5y\|2c5y]], [[2c68\|2c68]], [[2c69\|2c69]], [[2c6i\|2c6i]], [[2c6k\|2c6k]], [[2c6l\|2c6l]], [[2c6m\|2c6m]], [[2c6o\|2c6o]], [[2c6t\|2c6t]], [[2cch\|2cch]], [[2cci\|2cci]], [[2exm\|2exm]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </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=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [http://pdbe.org/2cjm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [http://www.ebi.ac.uk/pdbsum/2cjm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjm ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [http://pdbe.org/2cjm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [http://www.ebi.ac.uk/pdbsum/2cjm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 11:11, 26 February 2020

2020-02-26T11:11:33Z

←Older revision		Revision as of 11:11, 26 February 2020
Line 1:		Line 1:

	==Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure==		==Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure==
-	<StructureSection load='2cjm' size='340' side='right' caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='2cjm' size='340' side='right'caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJM FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJM FirstGlance]. <br>
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Cyclin\|Cyclin]]	+	*[[Cyclin 3D structures\|Cyclin 3D structures]]
-	*[[Cyclin-dependent kinase\|Cyclin-dependent kinase]]	+	*[[Cyclin-dependent kinase 3D structures\|Cyclin-dependent kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Endicott, J A]]		[[Category: Endicott, J A]]

OCA at 08:42, 23 May 2018

2018-05-23T08:42:30Z

←Older revision		Revision as of 08:42, 23 May 2018
Line 1:		Line 1:
		+
	==Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure==		==Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure==
	<StructureSection load='2cjm' size='340' side='right' caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2cjm' size='340' side='right' caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1okv\|1okv]], [[1okw\|1okw]], [[1ol1\|1ol1]], [[1ol2\|1ol2]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pf8\|1pf8]], [[1pkd\|1pkd]], [[1pw2\|1pw2]], [[1pxi\|1pxi]], [[1pxj\|1pxj]], [[1pxk\|1pxk]], [[1pxl\|1pxl]], [[1pxm\|1pxm]], [[1pxn\|1pxn]], [[1pxo\|1pxo]], [[1pxp\|1pxp]], [[1pye\|1pye]], [[1qmz\|1qmz]], [[1r78\|1r78]], [[1urc\|1urc]], [[1urw\|1urw]], [[1v1k\|1v1k]], [[1vyw\|1vyw]], [[1vyz\|1vyz]], [[1w0x\|1w0x]], [[1w8c\|1w8c]], [[1w98\|1w98]], [[1wcc\|1wcc]], [[1y8y\|1y8y]], [[1y91\|1y91]], [[1ykr\|1ykr]], [[2a0c\|2a0c]], [[2b52\|2b52]], [[2b53\|2b53]], [[2b54\|2b54]], [[2b55\|2b55]], [[2bhe\|2bhe]], [[2bhh\|2bhh]], [[2bkz\|2bkz]], [[2bpm\|2bpm]], [[2btr\|2btr]], [[2bts\|2bts]], [[2c4g\|2c4g]], [[2c5n\|2c5n]], [[2c5o\|2c5o]], [[2c5p\|2c5p]], [[2c5t\|2c5t]], [[2c5v\|2c5v]], [[2c5x\|2c5x]], [[2c5y\|2c5y]], [[2c68\|2c68]], [[2c69\|2c69]], [[2c6i\|2c6i]], [[2c6k\|2c6k]], [[2c6l\|2c6l]], [[2c6m\|2c6m]], [[2c6o\|2c6o]], [[2c6t\|2c6t]], [[2cch\|2cch]], [[2cci\|2cci]], [[2exm\|2exm]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1okv\|1okv]], [[1okw\|1okw]], [[1ol1\|1ol1]], [[1ol2\|1ol2]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pf8\|1pf8]], [[1pkd\|1pkd]], [[1pw2\|1pw2]], [[1pxi\|1pxi]], [[1pxj\|1pxj]], [[1pxk\|1pxk]], [[1pxl\|1pxl]], [[1pxm\|1pxm]], [[1pxn\|1pxn]], [[1pxo\|1pxo]], [[1pxp\|1pxp]], [[1pye\|1pye]], [[1qmz\|1qmz]], [[1r78\|1r78]], [[1urc\|1urc]], [[1urw\|1urw]], [[1v1k\|1v1k]], [[1vyw\|1vyw]], [[1vyz\|1vyz]], [[1w0x\|1w0x]], [[1w8c\|1w8c]], [[1w98\|1w98]], [[1wcc\|1wcc]], [[1y8y\|1y8y]], [[1y91\|1y91]], [[1ykr\|1ykr]], [[2a0c\|2a0c]], [[2b52\|2b52]], [[2b53\|2b53]], [[2b54\|2b54]], [[2b55\|2b55]], [[2bhe\|2bhe]], [[2bhh\|2bhh]], [[2bkz\|2bkz]], [[2bpm\|2bpm]], [[2btr\|2btr]], [[2bts\|2bts]], [[2c4g\|2c4g]], [[2c5n\|2c5n]], [[2c5o\|2c5o]], [[2c5p\|2c5p]], [[2c5t\|2c5t]], [[2c5v\|2c5v]], [[2c5x\|2c5x]], [[2c5y\|2c5y]], [[2c68\|2c68]], [[2c69\|2c69]], [[2c6i\|2c6i]], [[2c6k\|2c6k]], [[2c6l\|2c6l]], [[2c6m\|2c6m]], [[2c6o\|2c6o]], [[2c6t\|2c6t]], [[2cch\|2cch]], [[2cci\|2cci]], [[2exm\|2exm]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </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=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [http://www.ebi.ac.uk/pdbsum/2cjm 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=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [http://pdbe.org/2cjm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [http://www.ebi.ac.uk/pdbsum/2cjm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/2cjm_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/2cjm_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=2cjm ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	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 2cjm" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Cell division protein kinase\|Cell division protein kinase]]
	*[[Cyclin\|Cyclin]]		*[[Cyclin\|Cyclin]]
		+	*[[Cyclin-dependent kinase\|Cyclin-dependent kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:10, 1 April 2015

2015-04-01T07:10:04Z

←Older revision		Revision as of 07:10, 1 April 2015
Line 2:		Line 2:
	<StructureSection load='2cjm' size='340' side='right' caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2cjm' size='340' side='right' caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Cell division protein kinase 2\|Cell division protein kinase 2]]	+	*[[Cell division protein kinase\|Cell division protein kinase]]
	*[[Cyclin\|Cyclin]]		*[[Cyclin\|Cyclin]]
	== References ==		== References ==
Line 37:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Transferase]]		[[Category: Transferase]]
-	[[Category: Endicott, J. A]]	+	[[Category: Endicott, J A]]
	[[Category: Johnson, T]]		[[Category: Johnson, T]]
	[[Category: Lindert, L]]		[[Category: Lindert, L]]

OCA at 20:49, 25 December 2014

2014-12-25T20:49:17Z

←Older revision		Revision as of 20:49, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJM FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJM FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1okv\|1okv]], [[1okw\|1okw]], [[1ol1\|1ol1]], [[1ol2\|1ol2]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pf8\|1pf8]], [[1pkd\|1pkd]], [[1pw2\|1pw2]], [[1pxi\|1pxi]], [[1pxj\|1pxj]], [[1pxk\|1pxk]], [[1pxl\|1pxl]], [[1pxm\|1pxm]], [[1pxn\|1pxn]], [[1pxo\|1pxo]], [[1pxp\|1pxp]], [[1pye\|1pye]], [[1qmz\|1qmz]], [[1r78\|1r78]], [[1urc\|1urc]], [[1urw\|1urw]], [[1v1k\|1v1k]], [[1vyw\|1vyw]], [[1vyz\|1vyz]], [[1w0x\|1w0x]], [[1w8c\|1w8c]], [[1w98\|1w98]], [[1wcc\|1wcc]], [[1y8y\|1y8y]], [[1y91\|1y91]], [[1ykr\|1ykr]], [[2a0c\|2a0c]], [[2b52\|2b52]], [[2b53\|2b53]], [[2b54\|2b54]], [[2b55\|2b55]], [[2bhe\|2bhe]], [[2bhh\|2bhh]], [[2bkz\|2bkz]], [[2bpm\|2bpm]], [[2btr\|2btr]], [[2bts\|2bts]], [[2c4g\|2c4g]], [[2c5n\|2c5n]], [[2c5o\|2c5o]], [[2c5p\|2c5p]], [[2c5t\|2c5t]], [[2c5v\|2c5v]], [[2c5x\|2c5x]], [[2c5y\|2c5y]], [[2c68\|2c68]], [[2c69\|2c69]], [[2c6i\|2c6i]], [[2c6k\|2c6k]], [[2c6l\|2c6l]], [[2c6m\|2c6m]], [[2c6o\|2c6o]], [[2c6t\|2c6t]], [[2cch\|2cch]], [[2cci\|2cci]], [[2exm\|2exm]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1okv\|1okv]], [[1okw\|1okw]], [[1ol1\|1ol1]], [[1ol2\|1ol2]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pf8\|1pf8]], [[1pkd\|1pkd]], [[1pw2\|1pw2]], [[1pxi\|1pxi]], [[1pxj\|1pxj]], [[1pxk\|1pxk]], [[1pxl\|1pxl]], [[1pxm\|1pxm]], [[1pxn\|1pxn]], [[1pxo\|1pxo]], [[1pxp\|1pxp]], [[1pye\|1pye]], [[1qmz\|1qmz]], [[1r78\|1r78]], [[1urc\|1urc]], [[1urw\|1urw]], [[1v1k\|1v1k]], [[1vyw\|1vyw]], [[1vyz\|1vyz]], [[1w0x\|1w0x]], [[1w8c\|1w8c]], [[1w98\|1w98]], [[1wcc\|1wcc]], [[1y8y\|1y8y]], [[1y91\|1y91]], [[1ykr\|1ykr]], [[2a0c\|2a0c]], [[2b52\|2b52]], [[2b53\|2b53]], [[2b54\|2b54]], [[2b55\|2b55]], [[2bhe\|2bhe]], [[2bhh\|2bhh]], [[2bkz\|2bkz]], [[2bpm\|2bpm]], [[2btr\|2btr]], [[2bts\|2bts]], [[2c4g\|2c4g]], [[2c5n\|2c5n]], [[2c5o\|2c5o]], [[2c5p\|2c5p]], [[2c5t\|2c5t]], [[2c5v\|2c5v]], [[2c5x\|2c5x]], [[2c5y\|2c5y]], [[2c68\|2c68]], [[2c69\|2c69]], [[2c6i\|2c6i]], [[2c6k\|2c6k]], [[2c6l\|2c6l]], [[2c6m\|2c6m]], [[2c6o\|2c6o]], [[2c6t\|2c6t]], [[2cch\|2cch]], [[2cci\|2cci]], [[2exm\|2exm]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </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=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [http://www.ebi.ac.uk/pdbsum/2cjm 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=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [http://www.ebi.ac.uk/pdbsum/2cjm 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> [[http://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN]] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 39:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Transferase]]		[[Category: Transferase]]
-	[[Category: Endicott, J. A.]]	+	[[Category: Endicott, J. A]]
-	[[Category: Johnson, T.]]	+	[[Category: Johnson, T]]
-	[[Category: Lindert, L.]]	+	[[Category: Lindert, L]]
-	[[Category: Morgan, M.]]	+	[[Category: Morgan, M]]
-	[[Category: Noble, M E.M.]]	+	[[Category: Noble, M E.M]]
-	[[Category: Tucker, J.]]	+	[[Category: Tucker, J]]
-	[[Category: Welburn, J P.I.]]	+	[[Category: Welburn, J P.I]]
-	[[Category: Willis, A.]]	+	[[Category: Willis, A]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
Line 54:		Line 56:
	[[Category: Regulation]]		[[Category: Regulation]]
	[[Category: Serine/threonine-protein kinase]]		[[Category: Serine/threonine-protein kinase]]
-	[[Category: Transferase]]

OCA at 04:26, 3 October 2014

2014-10-03T04:26:47Z

←Older revision		Revision as of 04:26, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2cjm\| PDB=2cjm \| SCENE= }}~~	+	==Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure==
-	===Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure===	+	<StructureSection load='2cjm' size='340' side='right' caption='[[2cjm]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_17095507}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2cjm]] is a 4 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=2CJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJM FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1aq1\|1aq1]], [[1b38\|1b38]], [[1b39\|1b39]], [[1buh\|1buh]], [[1ckp\|1ckp]], [[1di8\|1di8]], [[1dm2\|1dm2]], [[1e1v\|1e1v]], [[1e1x\|1e1x]], [[1e9h\|1e9h]], [[1f5q\|1f5q]], [[1fin\|1fin]], [[1fq1\|1fq1]], [[1fvt\|1fvt]], [[1fvv\|1fvv]], [[1g5s\|1g5s]], [[1gih\|1gih]], [[1gii\|1gii]], [[1gij\|1gij]], [[1gy3\|1gy3]], [[1gz8\|1gz8]], [[1h00\|1h00]], [[1h01\|1h01]], [[1h07\|1h07]], [[1h08\|1h08]], [[1h0v\|1h0v]], [[1h0w\|1h0w]], [[1h1p\|1h1p]], [[1h1q\|1h1q]], [[1h1r\|1h1r]], [[1h1s\|1h1s]], [[1h24\|1h24]], [[1h25\|1h25]], [[1h26\|1h26]], [[1h27\|1h27]], [[1h28\|1h28]], [[1hck\|1hck]], [[1hcl\|1hcl]], [[1jst\|1jst]], [[1jsu\|1jsu]], [[1jsv\|1jsv]], [[1jvp\|1jvp]], [[1ke5\|1ke5]], [[1ke6\|1ke6]], [[1ke7\|1ke7]], [[1ke8\|1ke8]], [[1ke9\|1ke9]], [[1ogu\|1ogu]], [[1oi9\|1oi9]], [[1oiq\|1oiq]], [[1oir\|1oir]], [[1oit\|1oit]], [[1oiu\|1oiu]], [[1oiy\|1oiy]], [[1okv\|1okv]], [[1okw\|1okw]], [[1ol1\|1ol1]], [[1ol2\|1ol2]], [[1p2a\|1p2a]], [[1p5e\|1p5e]], [[1pf8\|1pf8]], [[1pkd\|1pkd]], [[1pw2\|1pw2]], [[1pxi\|1pxi]], [[1pxj\|1pxj]], [[1pxk\|1pxk]], [[1pxl\|1pxl]], [[1pxm\|1pxm]], [[1pxn\|1pxn]], [[1pxo\|1pxo]], [[1pxp\|1pxp]], [[1pye\|1pye]], [[1qmz\|1qmz]], [[1r78\|1r78]], [[1urc\|1urc]], [[1urw\|1urw]], [[1v1k\|1v1k]], [[1vyw\|1vyw]], [[1vyz\|1vyz]], [[1w0x\|1w0x]], [[1w8c\|1w8c]], [[1w98\|1w98]], [[1wcc\|1wcc]], [[1y8y\|1y8y]], [[1y91\|1y91]], [[1ykr\|1ykr]], [[2a0c\|2a0c]], [[2b52\|2b52]], [[2b53\|2b53]], [[2b54\|2b54]], [[2b55\|2b55]], [[2bhe\|2bhe]], [[2bhh\|2bhh]], [[2bkz\|2bkz]], [[2bpm\|2bpm]], [[2btr\|2btr]], [[2bts\|2bts]], [[2c4g\|2c4g]], [[2c5n\|2c5n]], [[2c5o\|2c5o]], [[2c5p\|2c5p]], [[2c5t\|2c5t]], [[2c5v\|2c5v]], [[2c5x\|2c5x]], [[2c5y\|2c5y]], [[2c68\|2c68]], [[2c69\|2c69]], [[2c6i\|2c6i]], [[2c6k\|2c6k]], [[2c6l\|2c6l]], [[2c6m\|2c6m]], [[2c6o\|2c6o]], [[2c6t\|2c6t]], [[2cch\|2cch]], [[2cci\|2cci]], [[2exm\|2exm]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </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=2cjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cjm RCSB], [http://www.ebi.ac.uk/pdbsum/2cjm PDBsum]</span></td></tr>
		+	<table>
		+	== 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/cj/2cjm_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Inhibition of cyclin-dependent kinase 1 (CDK1) activity by Tyr-15 phosphorylation directly regulates entry into mitosis and is an important element in the control of the unperturbed cell cycle. Active site phosphorylation of other members of the CDK family that regulate cell cycle progression instates checkpoints that are fundamental to eukaryotic cell cycle regulation. Kinetic and crystallographic analyses of CDK2-cyclin A complexes reveal that this inhibitory mechanism operates through steric blockade of peptide substrate binding and through the creation of an environment that favors a non-productive conformation of the terminal group of ATP. By contrast, tyrosine phosphorylation of CDK2 alters neither its Km for ATP nor its significant intrinsic ATPase activity. Tyr-15-phosphorylated CDK2 retains trace protein phosphorylation activity that should be considered in quantitative and qualitative cell cycle models.

-	~~==Function==~~	+	How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A.,Welburn JP, Tucker JA, Johnson T, Lindert L, Morgan M, Willis A, Noble ME, Endicott JA J Biol Chem. 2007 Feb 2;282(5):3173-81. Epub 2006 Nov 9. PMID:17095507<ref>PMID:17095507</ref>
-	~~[[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> [[http://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN]] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[2cjm]] is~~ a ~~4 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=2CJM OCA].~~	+	</div>

	==See Also==		==See Also==
-	*[[Cell ~~Division Protein Kinase~~ 2\|Cell ~~Division Protein Kinase~~ 2]]	+	*[[Cell division protein kinase 2\|Cell division protein kinase 2]]
	*[[Cyclin\|Cyclin]]		*[[Cyclin\|Cyclin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:017095507</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 14:29, 10 July 2013

2013-07-10T14:29:08Z

←Older revision		Revision as of 14:29, 10 July 2013
Line 1:		Line 1:
-	[[Image:2cjm.png\|left\|200px]]
-
	{{STRUCTURE_2cjm\| PDB=2cjm \| SCENE= }}		{{STRUCTURE_2cjm\| PDB=2cjm \| SCENE= }}
		+	===Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure===
		+	{{ABSTRACT_PUBMED_17095507}}

-	==~~=MECHANISM OF CDK INHIBITION BY ACTIVE SITE PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX WITH CYCLIN A STRUCTURE=~~==	+	==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> [[http://www.uniprot.org/uniprot/CCNA2_HUMAN CCNA2_HUMAN]] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.
-	~~{{ABSTRACT_PUBMED_17095507}}~~	+

	==About this Structure==		==About this Structure==
Line 15:		Line 14:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:017095507</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017095507</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: ~~Non-specific serine/threonine protein kinase~~]]	+	[[Category: Transferase]]
-	[[Category: Endicott, J A.]]	+	[[Category: Endicott, J. A.]]
	[[Category: Johnson, T.]]		[[Category: Johnson, T.]]
	[[Category: Lindert, L.]]		[[Category: Lindert, L.]]
		+	[[Category: Morgan, M.]]
	[[Category: Noble, M E.M.]]		[[Category: Noble, M E.M.]]
	[[Category: Tucker, J.]]		[[Category: Tucker, J.]]
Line 28:		Line 28:
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Cell division]]		[[Category: Cell division]]
-	[[Category: Cyclin]]
	[[Category: Cyclin-dependent kinase]]		[[Category: Cyclin-dependent kinase]]
-	[[Category: Kinase]]
	[[Category: Mitosis]]		[[Category: Mitosis]]
	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]

OCA at 21:27, 20 October 2012

2012-10-20T21:27:46Z

←Older revision		Revision as of 21:27, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2cjm]] is a 4 chain structure ~~of [[Cell Division Protein Kinase 2]] and [[Cyclin]]~~ 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=2CJM OCA].	+	[[2cjm]] is a 4 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=2CJM OCA].

	==See Also==		==See Also==

OCA: Protected "2cjm" [edit=sysop:move=sysop]

2012-07-27T13:20:11Z

Protected "2cjm" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:20, 27 July 2012