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==Crystal Structure of PRK1 Catalytic Domain==
==Crystal Structure of PRK1 Catalytic Domain==
<StructureSection load='4otd' size='340' side='right' caption='[[4otd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4otd' size='340' side='right'caption='[[4otd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4otd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OTD FirstGlance]. <br>
<table><tr><td colspan='2'>[[4otd]] 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=4OTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OTD FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4otg|4otg]], [[4oth|4oth]], [[4oti|4oti]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_kinase_C Protein kinase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.13 2.7.11.13] </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=4otd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4otd OCA], [https://pdbe.org/4otd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4otd RCSB], [https://www.ebi.ac.uk/pdbsum/4otd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4otd ProSAT]</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=4otd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4otd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4otd RCSB], [http://www.ebi.ac.uk/pdbsum/4otd PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PKN1_HUMAN PKN1_HUMAN]] PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.<ref>PMID:8557118</ref> <ref>PMID:8621664</ref> <ref>PMID:9175763</ref> <ref>PMID:11104762</ref> <ref>PMID:12514133</ref> <ref>PMID:17332740</ref> <ref>PMID:18066052</ref> <ref>PMID:20188095</ref> <ref>PMID:21754995</ref> 
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4otd" style="background-color:#fffaf0;"></div>
==See Also==
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Protein kinase C]]
[[Category: Homo sapiens]]
[[Category: Abbassian, M]]
[[Category: Large Structures]]
[[Category: B., Pagarigan]]
[[Category: Abbassian M]]
[[Category: Cathers, B]]
[[Category: Cathers B]]
[[Category: Chamberlain, P P]]
[[Category: Chamberlain PP]]
[[Category: Delker, S]]
[[Category: Delker S]]
[[Category: Jackson, P]]
[[Category: Jackson P]]
[[Category: Mahmoudi, A]]
[[Category: Mahmoudi A]]
[[Category: Muir, J]]
[[Category: Muir J]]
[[Category: Raheja, N]]
[[Category: Pagarigan B]]
[[Category: Atp binding]]
[[Category: Raheja N]]
[[Category: Kinase]]
[[Category: Phosphorylation]]
[[Category: Pkn1]]
[[Category: Prk1]]
[[Category: Protein kinase]]
[[Category: Protein kinase c related kinase 1]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/4otd"