3dxk: Difference between revisions

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-{{STRUCTURE_3dxk|  PDB=3dxk  |  SCENE=  }}
+==Structure of Bos Taurus Arp2/3 Complex with Bound Inhibitor CK0944636==
-===Structure of Bos Taurus Arp2/3 Complex with Bound Inhibitor CK0944636===
+<StructureSection load='3dxk' size='340' side='right' caption='[[3dxk]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-{{ABSTRACT_PUBMED_19648907}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3dxk]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DXK FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=N23:N-[2-(2-METHYL-1H-INDOL-3-YL)ETHYL]THIOPHENE-2-CARBOXAMIDE'>N23</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dxm|3dxm]]</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=3dxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dxk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dxk RCSB], [http://www.ebi.ac.uk/pdbsum/3dxk 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/dx/3dxk_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 ==
+Polymerization of actin filaments directed by the actin-related protein (Arp)2/3 complex supports many types of cellular movements. However, questions remain regarding the relative contributions of Arp2/3 complex versus other mechanisms of actin filament nucleation to processes such as path finding by neuronal growth cones; this is because of the lack of simple methods to inhibit Arp2/3 complex reversibly in living cells. Here we describe two classes of small molecules that bind to different sites on the Arp2/3 complex and inhibit its ability to nucleate actin filaments. CK-0944636 binds between Arp2 and Arp3, where it appears to block movement of Arp2 and Arp3 into their active conformation. CK-0993548 inserts into the hydrophobic core of Arp3 and alters its conformation. Both classes of compounds inhibit formation of actin filament comet tails by Listeria and podosomes by monocytes. Two inhibitors with different mechanisms of action provide a powerful approach for studying the Arp2/3 complex in living cells.
-==Function==
+Characterization of two classes of small molecule inhibitors of Arp2/3 complex.,Nolen BJ, Tomasevic N, Russell A, Pierce DW, Jia Z, McCormick CD, Hartman J, Sakowicz R, Pollard TD Nature. 2009 Aug 20;460(7258):1031-4. Epub 2009 Aug 2. PMID:19648907<ref>PMID:19648907</ref>
-[[http://www.uniprot.org/uniprot/ARPC4_BOVIN ARPC4_BOVIN]] Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity). [[http://www.uniprot.org/uniprot/ARPC2_BOVIN ARPC2_BOVIN]] Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity). [[http://www.uniprot.org/uniprot/ARP3_BOVIN ARP3_BOVIN]] Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. Plays a role in ciliogenesis (By similarity). [[http://www.uniprot.org/uniprot/ARC1B_BOVIN ARC1B_BOVIN]] Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (By similarity). [[http://www.uniprot.org/uniprot/ARPC5_BOVIN ARPC5_BOVIN]] Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (By similarity). [[http://www.uniprot.org/uniprot/ARP2_BOVIN ARP2_BOVIN]] Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. [[http://www.uniprot.org/uniprot/ARPC3_BOVIN ARPC3_BOVIN]] Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (By similarity).
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[3dxk]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DXK OCA].
+</div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:019648907</ref><references group="xtra"/><references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Hartman, J.]]
+[[Category: Hartman, J]]
-[[Category: Jia, Z.]]
+[[Category: Jia, Z]]
-[[Category: Nolen, B J.]]
+[[Category: Nolen, B J]]
-[[Category: Pierce, D W.]]
+[[Category: Pierce, D W]]
-[[Category: Pollard, T D.]]
+[[Category: Pollard, T D]]
-[[Category: Russell, A.]]
+[[Category: Russell, A]]
-[[Category: Sakowicz, R.]]
+[[Category: Sakowicz, R]]
-[[Category: Tomasevic, N.]]
+[[Category: Tomasevic, N]]
 [[Category: Actin-binding]]
 [[Category: Atp-binding]]