4igg: Difference between revisions

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{{STRUCTURE_4igg| PDB=4igg | SCENE= }}
==Full-length human alpha-catenin crystal structure==
===Full-length human alpha-catenin crystal structure===
<StructureSection load='4igg' size='340' side='right' caption='[[4igg]], [[Resolution|resolution]] 3.66&Aring;' scene=''>
{{ABSTRACT_PUBMED_23292143}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4igg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IGG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ehp|4ehp]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTNNA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4igg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4igg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4igg RCSB], [http://www.ebi.ac.uk/pdbsum/4igg PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CTNA1_HUMAN CTNA1_HUMAN]] 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The F-actin-binding cytoskeletal protein alpha-catenin interacts with beta-catenin-cadherin complexes and stabilizes cell-cell junctions. The beta-catenin-alpha-catenin complex cannot bind F-actin, whereas interactions of alpha-catenin with the cytoskeletal protein vinculin appear to be necessary to stabilize adherens junctions. Here we report the crystal structure of nearly full-length human alpha-catenin at 3.7-A resolution. alpha-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This results in a left handshake-like dimer, wherein the two subunits have remarkably different conformations. The crystal structure explains why dimeric alpha-catenin has a higher affinity for F-actin than does monomeric alpha-catenin, why the beta-catenin-alpha-catenin complex does not bind F-actin, how activated vinculin links the cadherin-catenin complex to the cytoskeleton and why alpha-catenin but not inactive vinculin can bind F-actin.


==Function==
Dimer asymmetry defines alpha-catenin interactions.,Rangarajan ES, Izard T Nat Struct Mol Biol. 2013 Feb;20(2):188-93. doi: 10.1038/nsmb.2479. Epub 2013 Jan, 6. PMID:23292143<ref>PMID:23292143</ref>
[[http://www.uniprot.org/uniprot/CTNA1_HUMAN CTNA1_HUMAN]] 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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4igg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGG OCA].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:023292143</ref><references group="xtra"/><references/>
*[[Catenin|Catenin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Izard, T.]]
[[Category: Izard, T]]
[[Category: Rangarajan, E S.]]
[[Category: Rangarajan, E S]]
[[Category: Adherens junction]]
[[Category: Adherens junction]]
[[Category: Asymmetric dimer]]
[[Category: Asymmetric dimer]]
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: F-actin binding]]
[[Category: F-actin binding]]

Revision as of 20:12, 24 December 2014

Full-length human alpha-catenin crystal structureFull-length human alpha-catenin crystal structure

Structural highlights

4igg is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:CTNNA1 (Homo sapiens)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[CTNA1_HUMAN] 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.

Publication Abstract from PubMed

The F-actin-binding cytoskeletal protein alpha-catenin interacts with beta-catenin-cadherin complexes and stabilizes cell-cell junctions. The beta-catenin-alpha-catenin complex cannot bind F-actin, whereas interactions of alpha-catenin with the cytoskeletal protein vinculin appear to be necessary to stabilize adherens junctions. Here we report the crystal structure of nearly full-length human alpha-catenin at 3.7-A resolution. alpha-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This results in a left handshake-like dimer, wherein the two subunits have remarkably different conformations. The crystal structure explains why dimeric alpha-catenin has a higher affinity for F-actin than does monomeric alpha-catenin, why the beta-catenin-alpha-catenin complex does not bind F-actin, how activated vinculin links the cadherin-catenin complex to the cytoskeleton and why alpha-catenin but not inactive vinculin can bind F-actin.

Dimer asymmetry defines alpha-catenin interactions.,Rangarajan ES, Izard T Nat Struct Mol Biol. 2013 Feb;20(2):188-93. doi: 10.1038/nsmb.2479. Epub 2013 Jan, 6. PMID:23292143[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Rangarajan ES, Izard T. Dimer asymmetry defines alpha-catenin interactions. Nat Struct Mol Biol. 2013 Feb;20(2):188-93. doi: 10.1038/nsmb.2479. Epub 2013 Jan, 6. PMID:23292143 doi:10.1038/nsmb.2479

4igg, resolution 3.66Å

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