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3p53

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==Structure of fascin==
==Structure of fascin==
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<StructureSection load='3p53' size='340' side='right' caption='[[3p53]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3p53' size='340' side='right'caption='[[3p53]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p53]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P53 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3p53]] 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=3P53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P53 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FAN1, FSCN1, HSN, Human, SNL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr>
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<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=3p53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p53 OCA], [http://pdbe.org/3p53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p53 RCSB], [http://www.ebi.ac.uk/pdbsum/3p53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p53 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p53 OCA], [https://pdbe.org/3p53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p53 RCSB], [https://www.ebi.ac.uk/pdbsum/3p53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p53 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FSCN1_HUMAN FSCN1_HUMAN]] Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration.<ref>PMID:9362073</ref> <ref>PMID:9571235</ref> <ref>PMID:20137952</ref> <ref>PMID:20393565</ref>
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[https://www.uniprot.org/uniprot/FSCN1_HUMAN FSCN1_HUMAN] Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration.<ref>PMID:9362073</ref> <ref>PMID:9571235</ref> <ref>PMID:20137952</ref> <ref>PMID:20393565</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fascin is the main actin filament bundling protein in filopodia. Because of the important role filopodia play in cell migration, fascin is emerging as a major target for cancer drug discovery. However, an understanding of the mechanism of bundle formation by fascin is critically lacking. Fascin consists of four beta-trefoil domains. Here, we show that fascin contains two major actin-binding sites, coinciding with regions of high sequence conservation in beta-trefoil domains 1 and 3. The site in beta-trefoil-1 is located near the binding site of the fascin inhibitor macroketone and comprises residue Ser-39, whose phosphorylation by protein kinase C down-regulates actin bundling and formation of filopodia. The site in beta-trefoil-3 is related by pseudo-2-fold symmetry to that in beta-trefoil-1. The two sites are approximately 5 nm apart, resulting in a distance between actin filaments in the bundle of approximately 8.1 nm. Residue mutations in both sites disrupt bundle formation in vitro as assessed by co-sedimentation with actin and electron microscopy and severely impair formation of filopodia in cells as determined by rescue experiments in fascin-depleted cells. Mutations of other areas of the fascin surface also affect actin bundling and formation of filopodia albeit to a lesser extent, suggesting that, in addition to the two major actin-binding sites, fascin makes secondary contacts with other filaments in the bundle. In a high resolution crystal structure of fascin, molecules of glycerol and polyethylene glycol are bound in pockets located within the two major actin-binding sites. These molecules could guide the rational design of new anticancer fascin inhibitors.
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Mechanism of actin filament bundling by fascin.,Jansen S, Collins A, Yang C, Rebowski G, Svitkina T, Dominguez R J Biol Chem. 2011 Aug 26;286(34):30087-96. Epub 2011 Jun 18. PMID:21685497<ref>PMID:21685497</ref>
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==See Also==
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*[[Fascin|Fascin]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3p53" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Dominguez, R]]
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[[Category: Large Structures]]
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[[Category: Jansen, S]]
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[[Category: Dominguez R]]
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[[Category: Beta-trefoil domain]]
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[[Category: Jansen S]]
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[[Category: Structural protein]]
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Current revision

Structure of fascin

PDB ID 3p53

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