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New page: left|200px<br /><applet load="1q1p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q1p, resolution 3.20Å" /> '''E-Cadherin activatio...
 
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[[Image:1q1p.gif|left|200px]]<br /><applet load="1q1p" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1q1p, resolution 3.20&Aring;" />
'''E-Cadherin activation'''<br />


==Overview==
==E-Cadherin activation==
Cellular adhesion by classical cadherins depends critically on the exact, proteolytic removal of their N-terminal prosequences. In this combined, solution NMR and X-ray crystallographic study, the consequences of, propeptide cleavage of an epithelial cadherin construct (domains 1 and 2), were followed at atomic level. At low protein concentration, the, N-terminal processing induces docking of the tryptophan-2 side-chain into, a binding pocket on the same molecule. At high concentration, cleavage, induces dimerization (KD=0.72 mM, k(off)=0.7 s(-1)) and concomitant, intermolecular exchange of the betaA-strands and the tryptophan-2, side-chains. Thus, the cleavage represents the switch from a nonadhesive, to the functional form of cadherin.
<StructureSection load='1q1p' size='340' side='right'caption='[[1q1p]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1q1p]] 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=1Q1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q1P 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]] 3.2&#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></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=1q1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1p OCA], [https://pdbe.org/1q1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q1p RCSB], [https://www.ebi.ac.uk/pdbsum/1q1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q1p 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/q1/1q1p_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=1q1p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cellular adhesion by classical cadherins depends critically on the exact proteolytic removal of their N-terminal prosequences. In this combined solution NMR and X-ray crystallographic study, the consequences of propeptide cleavage of an epithelial cadherin construct (domains 1 and 2) were followed at atomic level. At low protein concentration, the N-terminal processing induces docking of the tryptophan-2 side-chain into a binding pocket on the same molecule. At high concentration, cleavage induces dimerization (KD=0.72 mM, k(off)=0.7 s(-1)) and concomitant intermolecular exchange of the betaA-strands and the tryptophan-2 side-chains. Thus, the cleavage represents the switch from a nonadhesive to the functional form of cadherin.


==About this Structure==
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.,Haussinger D, Ahrens T, Aberle T, Engel J, Stetefeld J, Grzesiek S EMBO J. 2004 Apr 21;23(8):1699-708. Epub 2004 Apr 8. PMID:15071499<ref>PMID:15071499</ref>
1Q1P 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 CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q1P OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography., Haussinger D, Ahrens T, Aberle T, Engel J, Stetefeld J, Grzesiek S, EMBO J. 2004 Apr 21;23(8):1699-708. Epub 2004 Apr 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15071499 15071499]
</div>
<div class="pdbe-citations 1q1p" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cadherin 3D structures|Cadherin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Haussinger D]]
[[Category: Haussinger, D.]]
[[Category: Stetefeld J]]
[[Category: Stetefeld, J.]]
[[Category: CA]]
[[Category: cell-adhesion]]
 
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