4p9t: Difference between revisions
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==Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin== | ==Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin== | ||
<StructureSection load='4p9t' size='340' side='right' caption='[[4p9t]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4p9t' size='340' side='right' caption='[[4p9t]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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<table><tr><td colspan='2'>[[4p9t]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P9T FirstGlance]. <br> | <table><tr><td colspan='2'>[[4p9t]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P9T FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=4p9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p9t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p9t RCSB], [http://www.ebi.ac.uk/pdbsum/4p9t PDBsum]</span></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=4p9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p9t OCA], [http://pdbe.org/4p9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p9t RCSB], [http://www.ebi.ac.uk/pdbsum/4p9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p9t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4p9t" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Catenin|Catenin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 16:29, 19 April 2017
Structure of the free form of the N-terminal VH1 domain of monomeric alpha-cateninStructure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin
Structural highlights
Function[CTNA2_MOUSE] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.[1] [2] [3] Publication Abstract from PubMedThe N-terminal vinculin-homology 1 (VH1) domain of alpha-catenin facilitates two exclusive forms, a monomeric form directly bound to beta-catenin for linking E-cadherin to F-actin or a homodimer for the inhibition of beta-catenin binding. Competition of these two forms is affected by approximately 80 N-terminal residues, whose structure is poorly understood. We have determined the structure of the monomeric free form of the alphaN-catenin VH1 domain and revealed that the N-terminal residues form alpha1 and alpha2 helices to complete formation of the N-terminal four-helix bundle. Dynamic conformational changes of these two helices control formation of the beta-catenin-bound monomer or unbound homodimer. Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin.,Shibahara T, Hirano Y, Hakoshima T FEBS Lett. 2015 Jul 8;589(15):1754-60. doi: 10.1016/j.febslet.2015.05.053. Epub, 2015 Jun 9. PMID:26071377[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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