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| | <StructureSection load='3dxm' size='340' side='right'caption='[[3dxm]], [[Resolution|resolution]] 2.85Å' scene=''> | | <StructureSection load='3dxm' size='340' side='right'caption='[[3dxm]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dxm]] 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=3DXM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DXM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dxm]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DXM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=N24:(2S)-2-(3-BROMOPHENYL)-3-(5-CHLORO-2-HYDROXYPHENYL)-1,3-THIAZOLIDIN-4-ONE'>N24</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dxk|3dxk]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=N24:(2S)-2-(3-BROMOPHENYL)-3-(5-CHLORO-2-HYDROXYPHENYL)-1,3-THIAZOLIDIN-4-ONE'>N24</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3dxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dxm OCA], [http://pdbe.org/3dxm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dxm RCSB], [http://www.ebi.ac.uk/pdbsum/3dxm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dxm ProSAT]</span></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=3dxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dxm OCA], [https://pdbe.org/3dxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dxm RCSB], [https://www.ebi.ac.uk/pdbsum/3dxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dxm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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). | + | [https://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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3dxm" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3dxm" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Actin-related protein 3D structures|Actin-related protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hartman, J]] | + | [[Category: Hartman J]] |
| - | [[Category: Jia, Z]] | + | [[Category: Jia Z]] |
| - | [[Category: Nolen, B J]] | + | [[Category: Nolen BJ]] |
| - | [[Category: Pierce, D W]] | + | [[Category: Pierce DW]] |
| - | [[Category: Pollard, T D]] | + | [[Category: Pollard TD]] |
| - | [[Category: Russell, A]] | + | [[Category: Russell A]] |
| - | [[Category: Sakowicz, R]] | + | [[Category: Sakowicz R]] |
| - | [[Category: Tomasevic, N]] | + | [[Category: Tomasevic N]] |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
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).
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 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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nolen BJ, Tomasevic N, Russell A, Pierce DW, Jia Z, McCormick CD, Hartman J, Sakowicz R, Pollard TD. Characterization of two classes of small molecule inhibitors of Arp2/3 complex. Nature. 2009 Aug 20;460(7258):1031-4. Epub 2009 Aug 2. PMID:19648907 doi:10.1038/nature08231
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