3bqr

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==Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with an imidazo-pyridazine ligand==
==Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with an imidazo-pyridazine ligand==
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<StructureSection load='3bqr' size='340' side='right' caption='[[3bqr]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='3bqr' size='340' side='right'caption='[[3bqr]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3bqr]] 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=3BQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BQR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3bqr]] 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=3BQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BQR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4RB:4-(6-{[(1R)-1-(HYDROXYMETHYL)PROPYL]AMINO}IMIDAZO[1,2-B]PYRIDAZIN-3-YL)BENZOIC+ACID'>4RB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4RB:4-(6-{[(1R)-1-(HYDROXYMETHYL)PROPYL]AMINO}IMIDAZO[1,2-B]PYRIDAZIN-3-YL)BENZOIC+ACID'>4RB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAPK3, ZIPK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAPK3, ZIPK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
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<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=3bqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bqr OCA], [http://pdbe.org/3bqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bqr RCSB], [http://www.ebi.ac.uk/pdbsum/3bqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bqr ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bqr OCA], [https://pdbe.org/3bqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bqr RCSB], [https://www.ebi.ac.uk/pdbsum/3bqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bqr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DAPK3_HUMAN DAPK3_HUMAN]] Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation, actin cytoskeleton reorganization, cell motility, smooth muscle contraction, and mitosis, particularly cytokinesis. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A, and the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates STAT3 and enhances its transcriptional activity. Positively regulates the canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Can disrupt the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. Involved in the formation of promyelocytic leukemia protein nuclear body (PML-NB), one of many subnuclear domains in the eukaryotic cell nucleus, and which is involved in oncogenesis and viral infection. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, its association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition.<ref>PMID:10356987</ref> <ref>PMID:17126281</ref> <ref>PMID:12917339</ref> <ref>PMID:12560483</ref> <ref>PMID:15367680</ref> <ref>PMID:18995835</ref> <ref>PMID:16219639</ref> <ref>PMID:17158456</ref> <ref>PMID:18515077</ref> <ref>PMID:18084323</ref> <ref>PMID:21454679</ref> <ref>PMID:21408167</ref> Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B.<ref>PMID:10356987</ref> <ref>PMID:17126281</ref> <ref>PMID:12917339</ref> <ref>PMID:12560483</ref> <ref>PMID:15367680</ref> <ref>PMID:18995835</ref> <ref>PMID:16219639</ref> <ref>PMID:17158456</ref> <ref>PMID:18515077</ref> <ref>PMID:18084323</ref> <ref>PMID:21454679</ref> <ref>PMID:21408167</ref>
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[[https://www.uniprot.org/uniprot/DAPK3_HUMAN DAPK3_HUMAN]] Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation, actin cytoskeleton reorganization, cell motility, smooth muscle contraction, and mitosis, particularly cytokinesis. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A, and the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates STAT3 and enhances its transcriptional activity. Positively regulates the canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Can disrupt the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. Involved in the formation of promyelocytic leukemia protein nuclear body (PML-NB), one of many subnuclear domains in the eukaryotic cell nucleus, and which is involved in oncogenesis and viral infection. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, its association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition.<ref>PMID:10356987</ref> <ref>PMID:17126281</ref> <ref>PMID:12917339</ref> <ref>PMID:12560483</ref> <ref>PMID:15367680</ref> <ref>PMID:18995835</ref> <ref>PMID:16219639</ref> <ref>PMID:17158456</ref> <ref>PMID:18515077</ref> <ref>PMID:18084323</ref> <ref>PMID:21454679</ref> <ref>PMID:21408167</ref> Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B.<ref>PMID:10356987</ref> <ref>PMID:17126281</ref> <ref>PMID:12917339</ref> <ref>PMID:12560483</ref> <ref>PMID:15367680</ref> <ref>PMID:18995835</ref> <ref>PMID:16219639</ref> <ref>PMID:17158456</ref> <ref>PMID:18515077</ref> <ref>PMID:18084323</ref> <ref>PMID:21454679</ref> <ref>PMID:21408167</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/3bqr_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/3bqr_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>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bqr 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=3bqr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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==See Also==
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*[[Death-associated protein kinase 3D structures|Death-associated protein kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]

Revision as of 08:22, 19 January 2022

Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with an imidazo-pyridazine ligand

PDB ID 3bqr

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