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==The crystal structure of villin domain 6==
==The crystal structure of villin domain 6==
<StructureSection load='3fg7' size='340' side='right' caption='[[3fg7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3fg7' size='340' side='right'caption='[[3fg7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3fg7]] 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=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3fg7]] 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=3FG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FG7 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yu5|1yu5]], [[1p8x|1p8x]], [[1nph|1nph]]</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&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VIL, VIL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [https://pdbe.org/3fg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [https://www.ebi.ac.uk/pdbsum/3fg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fg7 ProSAT]</span></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=3fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg7 OCA], [http://pdbe.org/3fg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg7 PDBsum]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.  
[https://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN] Note=Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN]] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>PMID:3087992</ref> <ref>PMID:11500485</ref> <ref>PMID:14594952</ref> <ref>PMID:15084600</ref> <ref>PMID:15272027</ref> <ref>PMID:15342783</ref> <ref>PMID:16921170</ref> <ref>PMID:17229814</ref> <ref>PMID:17606613</ref> <ref>PMID:17182858</ref> <ref>PMID:18054784</ref> <ref>PMID:18198174</ref> <ref>PMID:19808673</ref>
[https://www.uniprot.org/uniprot/VILI_HUMAN VILI_HUMAN] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.<ref>PMID:3087992</ref> <ref>PMID:11500485</ref> <ref>PMID:14594952</ref> <ref>PMID:15084600</ref> <ref>PMID:15272027</ref> <ref>PMID:15342783</ref> <ref>PMID:16921170</ref> <ref>PMID:17229814</ref> <ref>PMID:17606613</ref> <ref>PMID:17182858</ref> <ref>PMID:18054784</ref> <ref>PMID:18198174</ref> <ref>PMID:19808673</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/3fg7_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/3fg7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Burtnick, L D]]
[[Category: Large Structures]]
[[Category: Robinson, R C]]
[[Category: Burtnick LD]]
[[Category: Wang, H]]
[[Category: Robinson RC]]
[[Category: Actin binding protein]]
[[Category: Wang H]]
[[Category: Actin capping]]
[[Category: Actin-binding]]
[[Category: Cytoskeleton]]
[[Category: Gelsolin]]
[[Category: Structural protein]]
[[Category: Villin]]
[[Category: Villin head piece]]

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