4equ: Difference between revisions
New page: '''Unreleased structure''' The entry 4equ is ON HOLD Authors: Merritt, E.A., Larson, E.T. Description: HUMAN STK-10 (LOK) KINASE DOMAIN BOUND TO DSA-7 |
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The entry | ==Human STK-10 (LOK) kinase domain in DFG-out conformation with inhibitor DSA-7== | ||
<StructureSection load='4equ' size='340' side='right'caption='[[4equ]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4equ]] is a 2 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=4EQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EQU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=G6I:N-{3-[(3-{4-[(4-METHOXYPHENYL)AMINO]-1,3,5-TRIAZIN-2-YL}PYRIDIN-2-YL)AMINO]-4-METHYLPHENYL}-3-(TRIFLUOROMETHYL)BENZAMIDE'>G6I</scene></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=4equ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4equ OCA], [https://pdbe.org/4equ PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4equ RCSB], [https://www.ebi.ac.uk/pdbsum/4equ PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4equ ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/STK10_HUMAN STK10_HUMAN] The disease may be caused by mutations affecting the gene represented in this entry.<ref>PMID:16175573</ref> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/STK10_HUMAN STK10_HUMAN] Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.<ref>PMID:11903060</ref> <ref>PMID:12639966</ref> <ref>PMID:19255442</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein kinases are key components of most mammalian signal transduction networks and are therapeutically relevant drug targets. Efforts to study protein kinase function would benefit from new technologies that are able to profile kinases in complex proteomes. Here, we describe active site-directed probes for profiling kinases in whole cell extracts and live cells. These probes contain general ligands that stabilize a specific inactive conformation of the ATP-binding sites of protein kinases, as well as trifluoromethylphenyl diazirine and alkyne moieties that allow covalent modification and enrichment of kinases, respectively. A diverse group of serine/threonine and tyrosine kinases were identified as specific targets of these probes in whole cell extracts. In addition, a number of kinase targets were selectively labeled in live cells. Our chemical proteomics approach should be valuable for interrogating protein kinase active sites in physiologically relevant environments. | |||
Affinity-Based Probes Based on Type II Kinase Inhibitors.,Ranjitkar P, Perera BG, Swaney DL, Hari SB, Larson ET, Krishnamurty R, Merritt EA, Villen J, Maly DJ J Am Chem Soc. 2012 Nov 6. PMID:23088519<ref>PMID:23088519</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4equ" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Larson ET]] | |||
[[Category: Merritt EA]] | |||
Latest revision as of 09:56, 27 November 2024
Human STK-10 (LOK) kinase domain in DFG-out conformation with inhibitor DSA-7Human STK-10 (LOK) kinase domain in DFG-out conformation with inhibitor DSA-7
Structural highlights
DiseaseSTK10_HUMAN The disease may be caused by mutations affecting the gene represented in this entry.[1] FunctionSTK10_HUMAN Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.[2] [3] [4] Publication Abstract from PubMedProtein kinases are key components of most mammalian signal transduction networks and are therapeutically relevant drug targets. Efforts to study protein kinase function would benefit from new technologies that are able to profile kinases in complex proteomes. Here, we describe active site-directed probes for profiling kinases in whole cell extracts and live cells. These probes contain general ligands that stabilize a specific inactive conformation of the ATP-binding sites of protein kinases, as well as trifluoromethylphenyl diazirine and alkyne moieties that allow covalent modification and enrichment of kinases, respectively. A diverse group of serine/threonine and tyrosine kinases were identified as specific targets of these probes in whole cell extracts. In addition, a number of kinase targets were selectively labeled in live cells. Our chemical proteomics approach should be valuable for interrogating protein kinase active sites in physiologically relevant environments. Affinity-Based Probes Based on Type II Kinase Inhibitors.,Ranjitkar P, Perera BG, Swaney DL, Hari SB, Larson ET, Krishnamurty R, Merritt EA, Villen J, Maly DJ J Am Chem Soc. 2012 Nov 6. PMID:23088519[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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