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New page: left|200px<br /><applet load="1edh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1edh, resolution 2.0Å" /> '''E-CADHERIN DOMAINS 1 ...
 
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[[Image:1edh.gif|left|200px]]<br /><applet load="1edh" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1edh, resolution 2.0&Aring;" />
'''E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM'''<br />


==Overview==
==E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM==
The cadherins mediate cell adhesion and play a fundamental role in normal, development. They participate in the maintenance of proper cell-cell, contacts: for example, reduced levels of epithelial cadherin (E-cadherin), correlate with increased invasiveness in many human tumour cell types. The, cadherins typically consist of five tandemly repeated extracellular, domains, a single membrane-spanning segment and a cytoplasmic region. The, N-terminal extracellular domains mediate cell-cell contact while the, cytoplasmic region interacts with the cytoskeleton through the catenins., Cadherins depend on calcium for their function: removal of calcium, abolishes adhesive activity, renders cadherins vulnerable to proteases, (reviewed in ref. 4) and, in E-cadherin, induces a dramatic reversible, conformational change in the entire extracellular region. We report here, the X-ray crystal structure at 2.0 A resolution of the two N-terminal, extracellular domains of E-cadherin in the presence of calcium. The, structure reveals a two-fold symmetric dimer, each molecule of which binds, a contiguous array of three bridged calcium ions. Not only do the bound, calcium ions linearize and rigidify the molecule, they promote, dimerization. Although the N-terminal domain of each molecule in the dimer, is aligned in a parallel orientation, the interactions between them differ, significantly from those found in the neural cadherin (N-cadherin), N-terminal domain (NCD1) structure. The E-cadherin dual-domain structure, reported here defines the role played by calcium in the cadherin-mediated, formation and maintenance of solid tissues.
<StructureSection load='1edh' size='340' side='right'caption='[[1edh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1edh]] is a 2 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=1EDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1edh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edh OCA], [https://pdbe.org/1edh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edh RCSB], [https://www.ebi.ac.uk/pdbsum/1edh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CADH1_MOUSE CADH1_MOUSE] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity). E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/1edh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1edh ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with HG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EDH OCA].
*[[Cadherin 3D structures|Cadherin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis of calcium-induced E-cadherin rigidification and dimerization., Nagar B, Overduin M, Ikura M, Rini JM, Nature. 1996 Mar 28;380(6572):360-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8598933 8598933]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Ikura M]]
[[Category: Ikura, M.]]
[[Category: Nagar B]]
[[Category: Nagar, B.]]
[[Category: Overduin M]]
[[Category: Overduin, M.]]
[[Category: Rini JM]]
[[Category: Rini, J.M.]]
[[Category: CA]]
[[Category: HG]]
[[Category: cadherin]]
[[Category: calcium binding protein]]
[[Category: cell adhesion protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:55:07 2007''

Latest revision as of 07:01, 7 February 2024

E-CADHERIN DOMAINS 1 AND 2 IN COMPLEX WITH CALCIUM

1edh, resolution 2.00Å

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