2c30: Difference between revisions

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-{{Seed}}
-[[Image:2c30.png|left|200px]]
-<!--
+==Crystal Structure Of The Human P21-Activated Kinase 6==
-The line below this paragraph, containing "STRUCTURE_2c30", creates the "Structure Box" on the page.
+<StructureSection load='2c30' size='340' side='right'caption='[[2c30]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2c30]] 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=2C30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C30 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
-{{STRUCTURE_2c30|  PDB=2c30  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c30 OCA], [https://pdbe.org/2c30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c30 RCSB], [https://www.ebi.ac.uk/pdbsum/2c30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c30 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PAK6_HUMAN PAK6_HUMAN] Serine/threonine protein kinase that plays a role in the regulation of gene transcription. The kinase activity is induced by various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the DNA-binding domain of androgen receptor/AR and thereby inhibits AR-mediated transcription. Inhibits also ESR1-mediated transcription. May play a role in cytoskeleton regulation by interacting with IQGAP1. May protect cells from apoptosis through phosphorylation of BAD.<ref>PMID:14573606</ref> <ref>PMID:20054820</ref>
+== 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/c3/2c30_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2c30 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+p21-activated kinases have been classified into two groups based on their domain architecture. Group II PAKs (PAK4-6) regulate a wide variety of cellular functions, and PAK deregulation has been linked to tumor development. Structural comparison of five high-resolution structures comprising all active, monophosphorylated group II catalytic domains revealed a surprising degree of domain plasticity, including a number of catalytically productive and nonproductive conformers. Rearrangements of helix alphaC, a key regulatory element of kinase function, resulted in an additional helical turn at the alphaC N terminus and a distortion of its C terminus, a movement hitherto unseen in protein kinases. The observed structural changes led to the formation of interactions between conserved residues that structurally link the glycine-rich loop, alphaC, and the activation segment and firmly anchor alphaC in an active conformation. Inhibitor screening identified six potent PAK inhibitors from which a tri-substituted purine inhibitor was cocrystallized with PAK4 and PAK5.
-===CRYSTAL STRUCTURE OF THE HUMAN P21-ACTIVATED KINASE 6===
+Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs.,Eswaran J, Lee WH, Debreczeni JE, Filippakopoulos P, Turnbull A, Fedorov O, Deacon SW, Peterson JR, Knapp S Structure. 2007 Feb;15(2):201-13. PMID:17292838<ref>PMID:17292838</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2c30" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17292838}}, adds the Publication Abstract to the page
+*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17292838 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17292838}}
+__TOC__
+</StructureSection>
-==About this Structure==
-C30 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C30 OCA].
-==Reference==
-Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs., Eswaran J, Lee WH, Debreczeni JE, Filippakopoulos P, Turnbull A, Fedorov O, Deacon SW, Peterson JR, Knapp S, Structure. 2007 Feb;15(2):201-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17292838 17292838]
 [[Category: Homo sapiens]]
-[[Category: Non-specific serine/threonine protein kinase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Arrowsmith C]]
-[[Category: Arrowsmith, C.]]
+[[Category: Berridge G]]
-[[Category: Berridge, G.]]
+[[Category: Bray J]]
-[[Category: Bray, J.]]
+[[Category: Burgess N]]
-[[Category: Burgess, N.]]
+[[Category: Colebrook S]]
-[[Category: Colebrook, S.]]
+[[Category: Das S]]
-[[Category: Das, S.]]
+[[Category: Edwards A]]
-[[Category: Delft, F Von.]]
+[[Category: Eswaran J]]
-[[Category: Edwards, A.]]
+[[Category: Filippakopoulos P]]
-[[Category: Eswaran, J.]]
+[[Category: Gileadi O]]
-[[Category: Filippakopoulos, P.]]
+[[Category: Knapp S]]
-[[Category: Gileadi, O.]]
+[[Category: Papagrigoriou E]]
-[[Category: Knapp, S.]]
+[[Category: Savitsky P]]
-[[Category: Papagrigoriou, E.]]
+[[Category: Smee C]]
-[[Category: Savitsky, P.]]
+[[Category: Sundstrom M]]
-[[Category: Smee, C.]]
+[[Category: Turnbull A]]
-[[Category: Sundstrom, M.]]
+[[Category: Weigelt J]]
-[[Category: Turnbull, A.]]
+[[Category: Von Delft F]]
-[[Category: Weigelt, J.]]
-[[Category: Atp-binding]]
-[[Category: Crib domain]]
-[[Category: Kinase]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphorylation]]
-[[Category: Polymorphism]]
-[[Category: Serine-threonine protein kinase]]
-[[Category: Ste20-like]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:13:15 2008''