4cz3: Difference between revisions

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==HP24wt derived from the villin headpiece subdomain==
==HP24wt derived from the villin headpiece subdomain==
<StructureSection load='4cz3' size='340' side='right' caption='[[4cz3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='4cz3' size='340' side='right'caption='[[4cz3]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4cz3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CZ3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4cz3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CZ3 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cz4|4cz4]]</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=4cz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cz3 OCA], [https://pdbe.org/4cz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cz3 RCSB], [https://www.ebi.ac.uk/pdbsum/4cz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cz3 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=4cz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cz3 OCA], [http://pdbe.org/4cz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cz3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cz3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VILI_CHICK VILI_CHICK]] 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 (By similarity). Its actin-bundling activity is inhibited by tropomyosin.<ref>PMID:3793760</ref> <ref>PMID:1618806</ref>
[https://www.uniprot.org/uniprot/VILI_CHICK VILI_CHICK] 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 (By similarity). Its actin-bundling activity is inhibited by tropomyosin.<ref>PMID:3793760</ref> <ref>PMID:1618806</ref>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Haese, F]]
[[Category: Gallus gallus]]
[[Category: Hocking, H]]
[[Category: Large Structures]]
[[Category: Madl, T]]
[[Category: Haese F]]
[[Category: Rief, M]]
[[Category: Hocking H]]
[[Category: Zacharias, M]]
[[Category: Madl T]]
[[Category: Zoldak, G]]
[[Category: Rief M]]
[[Category: Actin-binding protein]]
[[Category: Zacharias M]]
[[Category: Supersecondary]]
[[Category: Zoldak G]]

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