3trw: Difference between revisions

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[[Image:3trw.png|left|200px]]


{{STRUCTURE_3trw|  PDB=3trw  |  SCENE=  }}
==Crystal structure of racemic villin headpiece subdomain crystallized in space group P-1==
 
<StructureSection load='3trw' size='340' side='right'caption='[[3trw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
===Crystal structure of racemic villin headpiece subdomain crystallized in space group P-1===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3trw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TRW FirstGlance]. <br>
{{ABSTRACT_PUBMED_22280019}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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=3trw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3trw OCA], [https://pdbe.org/3trw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3trw RCSB], [https://www.ebi.ac.uk/pdbsum/3trw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3trw ProSAT]</span></td></tr>
==About this Structure==
</table>
[[3trw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TRW OCA].  
== Function ==
[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>


==See Also==
==See Also==
*[[Villin|Villin]]
*[[Villin|Villin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:022280019</ref><references group="xtra"/>
__TOC__
[[Category: Forest, K T.]]
</StructureSection>
[[Category: Gellman, S H.]]
[[Category: Gallus gallus]]
[[Category: Mortenson, D E.]]
[[Category: Large Structures]]
[[Category: Satyshur, K A.]]
[[Category: Forest KT]]
[[Category: D-amino acid]]
[[Category: Gellman SH]]
[[Category: Quasi-racemate]]
[[Category: Mortenson DE]]
[[Category: Racemate]]
[[Category: Satyshur KA]]
[[Category: Structural protein]]