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[[Image: | ==Crystal structures of the kinase domain of PKA in complex with ATP-competitive inhibitors== | ||
<StructureSection load='3e8e' size='340' side='right' caption='[[3e8e]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3e8e]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E8E FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G98:4-[2-(4-AMINO-2,5-DIHYDRO-1,2,5-OXADIAZOL-3-YL)-6-{[(1S)-3-AMINO-1-PHENYLPROPYL]OXY}-1-ETHYL-1H-IMIDAZO[4,5-C]PYRIDIN-4-YL]-2-METHYLBUT-3-YN-2-OL'>G98</scene></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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e87|3e87]], [[3e88|3e88]], [[3e8c|3e8c]], [[3e8d|3e8d]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PKA, PRKACA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] </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=3e8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e8e RCSB], [http://www.ebi.ac.uk/pdbsum/3e8e 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/e8/3e8e_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 == | |||
AKT inhibitors containing an imidazopyridine aminofurazan scaffold have been optimized. We have previously disclosed identification of the AKT inhibitor GSK690693, which has been evaluated in clinical trials in cancer patients. Herein we describe recent efforts focusing on investigating a distinct region of this scaffold that have afforded compounds (30 and 32) with comparable activity profiles to that of GSK690693. | |||
Aminofurazans as potent inhibitors of AKT kinase.,Rouse MB, Seefeld MA, Leber JD, McNulty KC, Sun L, Miller WH, Zhang S, Minthorn EA, Concha NO, Choudhry AE, Schaber MD, Heerding DA Bioorg Med Chem Lett. 2009 Mar 1;19(5):1508-11. Epub 2009 Jan 9. PMID:19179070<ref>PMID:19179070</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[CAMP-dependent protein kinase|CAMP-dependent protein kinase]] | *[[CAMP-dependent protein kinase|CAMP-dependent protein kinase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Bovin]] | |||
[[Category: CAMP-dependent protein kinase]] | [[Category: CAMP-dependent protein kinase]] | ||
[[Category: Concha, N O | [[Category: Concha, N O]] | ||
[[Category: Elkins, P A | [[Category: Elkins, P A]] | ||
[[Category: Smallwood, A | [[Category: Smallwood, A]] | ||
[[Category: Ward, P | [[Category: Ward, P]] | ||
[[Category: Akt2]] | [[Category: Akt2]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
Revision as of 13:31, 19 November 2014
Crystal structures of the kinase domain of PKA in complex with ATP-competitive inhibitorsCrystal structures of the kinase domain of PKA in complex with ATP-competitive inhibitors
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAKT inhibitors containing an imidazopyridine aminofurazan scaffold have been optimized. We have previously disclosed identification of the AKT inhibitor GSK690693, which has been evaluated in clinical trials in cancer patients. Herein we describe recent efforts focusing on investigating a distinct region of this scaffold that have afforded compounds (30 and 32) with comparable activity profiles to that of GSK690693. Aminofurazans as potent inhibitors of AKT kinase.,Rouse MB, Seefeld MA, Leber JD, McNulty KC, Sun L, Miller WH, Zhang S, Minthorn EA, Concha NO, Choudhry AE, Schaber MD, Heerding DA Bioorg Med Chem Lett. 2009 Mar 1;19(5):1508-11. Epub 2009 Jan 9. PMID:19179070[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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