1dov: Difference between revisions

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


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==CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN==
The line below this paragraph, containing "STRUCTURE_1dov", creates the "Structure Box" on the page.
<StructureSection load='1dov' size='340' side='right'caption='[[1dov]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1dov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOV 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]] 3&#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=1dov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dov OCA], [https://pdbe.org/1dov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dov RCSB], [https://www.ebi.ac.uk/pdbsum/1dov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dov ProSAT]</span></td></tr>
{{STRUCTURE_1dov|  PDB=1dov  |  SCENE=  }}
</table>
 
== Function ==
===CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN===
[https://www.uniprot.org/uniprot/CTNA1_MOUSE CTNA1_MOUSE] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.<ref>PMID:16325583</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=1dov ConSurf].
[[1dov]] is a 1 chain structure of [[Catenin]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOV OCA].  
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==See Also==
==See Also==
*[[Catenin]]
*[[Catenin 3D structures|Catenin 3D structures]]
 
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
==Reference==
== References ==
<ref group="xtra">PMID:10882138</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Pokutta, S.]]
[[Category: Pokutta S]]
[[Category: Weis, W I.]]
[[Category: Weis WI]]
[[Category: Cell adhesion]]
[[Category: Four-helix bundle]]

Latest revision as of 09:57, 7 February 2024

CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAINCRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN

Structural highlights

1dov is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CTNA1_MOUSE Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.[1]

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. ↑ Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI. Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell. 2005 Dec 2;123(5):903-15. PMID:16325583 doi:10.1016/j.cell.2005.09.021

1dov, resolution 3.00Å

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