4igg

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==Full-length human alpha-catenin crystal structure==
==Full-length human alpha-catenin crystal structure==
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<StructureSection load='4igg' size='340' side='right' caption='[[4igg]], [[Resolution|resolution]] 3.66&Aring;' scene=''>
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<StructureSection load='4igg' size='340' side='right'caption='[[4igg]], [[Resolution|resolution]] 3.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4igg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
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<table><tr><td colspan='2'>[[4igg]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4IGG FirstGlance]. <br>
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</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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ehp|4ehp]]</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=4igg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4igg OCA], [https://pdbe.org/4igg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4igg RCSB], [https://www.ebi.ac.uk/pdbsum/4igg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4igg ProSAT]</span></td></tr>
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<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 HUMAN])</td></tr>
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<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://pdbe.org/4igg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4igg RCSB], [http://www.ebi.ac.uk/pdbsum/4igg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4igg ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Catenin|Catenin]]
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*[[Catenin 3D structures|Catenin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Izard, T]]
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[[Category: Large Structures]]
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[[Category: Rangarajan, E S]]
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[[Category: Izard T]]
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[[Category: Adherens junction]]
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[[Category: Rangarajan ES]]
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[[Category: Asymmetric dimer]]
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[[Category: Cell adhesion]]
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[[Category: F-actin binding]]
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Revision as of 20:43, 16 November 2022

Full-length human alpha-catenin crystal structure

PDB ID 4igg

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