4otd
From Proteopedia
(Difference between revisions)
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== 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. 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> | ||
| - | </td></tr><tr><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='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> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4otg|4otg]], [[4oth|4oth]], [[4oti|4oti]]</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><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='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><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> | + | <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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</StructureSection> | </StructureSection> | ||
[[Category: Protein kinase C]] | [[Category: Protein kinase C]] | ||
| - | [[Category: Abbassian, M | + | [[Category: Abbassian, M]] |
| - | [[Category: B., Pagarigan | + | [[Category: B., Pagarigan]] |
| - | [[Category: Cathers, B | + | [[Category: Cathers, B]] |
| - | [[Category: Chamberlain, P P | + | [[Category: Chamberlain, P P]] |
| - | [[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: Raheja, N]] |
[[Category: Atp binding]] | [[Category: Atp binding]] | ||
[[Category: Kinase]] | [[Category: Kinase]] | ||
Revision as of 18:40, 25 December 2014
Crystal Structure of PRK1 Catalytic Domain
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