1yu8: Difference between revisions

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[[Image:1yu8.png|left|200px]]


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==Crystal Structure of the R37A Mutant of Villin Headpiece==
The line below this paragraph, containing "STRUCTURE_1yu8", creates the "Structure Box" on the page.
<StructureSection load='1yu8' size='340' side='right'caption='[[1yu8]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1yu8]] is a 1 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=1YU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YU8 FirstGlance]. <br>
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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]] 1.45&#8491;</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=1yu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yu8 OCA], [https://pdbe.org/1yu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yu8 RCSB], [https://www.ebi.ac.uk/pdbsum/1yu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yu8 ProSAT]</span></td></tr>
{{STRUCTURE_1yu8|  PDB=1yu8  |  SCENE=  }}
</table>
 
== Function ==
===Crystal Structure of the R37A Mutant of Villin Headpiece===
[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>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
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==About this Structure==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yu8 ConSurf].
[[1yu8]] is a 1 chain structure of [[Villin]] with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YU8 OCA].  
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Villin]]
*[[Villin|Villin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:16142894</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Guo, H C.]]
[[Category: Large Structures]]
[[Category: Head, J F.]]
[[Category: Guo HC]]
[[Category: McKnight, C J.]]
[[Category: Head JF]]
[[Category: Meng, J.]]
[[Category: McKnight CJ]]
[[Category: Vardar, D.]]
[[Category: Meng J]]
[[Category: Wang, Y.]]
[[Category: Vardar D]]
[[Category: 3-10 helix]]
[[Category: Wang Y]]
[[Category: Alpha helix]]
[[Category: Structural protein]]

Latest revision as of 12:00, 14 February 2024

Crystal Structure of the R37A Mutant of Villin HeadpieceCrystal Structure of the R37A Mutant of Villin Headpiece

Structural highlights

1yu8 is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.45Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Burgess DR, Broschat KO, Hayden JM. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. J Cell Biol. 1987 Jan;104(1):29-40. PMID:3793760
  2. ↑ de Arruda MV, Bazari H, Wallek M, Matsudaira P. An actin footprint on villin. Single site substitutions in a cluster of basic residues inhibit the actin severing but not capping activity of villin. J Biol Chem. 1992 Jun 25;267(18):13079-85. PMID:1618806

1yu8, resolution 1.45Å

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