4oth: Difference between revisions
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''' | ==Crystal Structure of PRK1 Catalytic Domain in Complex with Ro-31-8220== | ||
<StructureSection load='4oth' size='340' side='right' caption='[[4oth]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4oth]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OTH FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DRN:BISINDOLYLMALEIMIDE+IX'>DRN</scene><br> | |||
<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> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4otd|4otd]], [[4otg|4otg]], [[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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oth OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oth RCSB], [http://www.ebi.ac.uk/pdbsum/4oth PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein kinase C related kinase 1 (PRK1) is a component of Rho-GTPase, androgen receptor, histone demethylase and histone deacetylase signaling pathways implicated in prostate and ovarian cancer. Herein we describe the crystal structure of PRK1 in apo form, and also in complex with a panel of literature inhibitors including the clinical candidates lestaurtinib and tofacitinib, as well as the staurosporine analog Ro-31-8220. PRK1 is a member of the AGC-kinase class, and as such exhibits the characteristic regulatory sequence at the C-terminus of the catalytic domain - the 'C-tail'. The C-tail fully encircles the catalytic domain placing a phenylalanine in the ATP-binding site. Our inhibitor structures include examples of molecules which both interact with, and displace the C-tail from the active site. This information may assist in the design of inhibitors targeting both PRK and other members of the AGC kinase family. | |||
Crystal Structures of PRK1 in Complex with the Clinical Compounds Lestaurtinib and Tofacitinib Reveal Ligand Induced Conformational Changes.,Chamberlain P, Delker S, Pagarigan B, Mahmoudi A, Jackson P, Abbasian M, Muir J, Raheja N, Cathers B PLoS One. 2014 Aug 11;9(8):e103638. doi: 10.1371/journal.pone.0103638., eCollection 2014. PMID:25111382<ref>PMID:25111382</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Protein kinase C]] | |||
[[Category: Abbassian, M.]] | |||
[[Category: B., Pagarigan.]] | |||
[[Category: Cathers, B.]] | |||
[[Category: Chamberlain, P P.]] | |||
[[Category: Delker, S.]] | |||
[[Category: Jackson, P.]] | |||
[[Category: Mahmoudi, A.]] | |||
[[Category: Muir, J.]] | |||
[[Category: Raheja, N.]] | |||
[[Category: Atp binding]] | |||
[[Category: Kinase]] | |||
[[Category: Phosphorylation]] | |||
[[Category: Pkn1]] | |||
[[Category: Prk1]] | |||
[[Category: Protein kinase]] | |||
[[Category: Protein kinase c related kinase 1]] | |||
[[Category: Transferase-transferase inhibitor complex]] | |||