2a4c: Difference between revisions

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[[Image:2a4c.gif|left|200px]]
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{{STRUCTURE_2a4c|  PDB=2a4c  |  SCENE=  }}
'''Crystal structure of mouse cadherin-11 EC1'''


==Crystal structure of mouse cadherin-11 EC1==
<StructureSection load='2a4c' size='340' side='right'caption='[[2a4c]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2a4c]] 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=2A4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A4C 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]] 2.9&#8491;</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=2a4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a4c OCA], [https://pdbe.org/2a4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a4c RCSB], [https://www.ebi.ac.uk/pdbsum/2a4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a4c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAD11_MOUSE CAD11_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.
== 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/a4/2a4c_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=2a4c ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type I and II classical cadherins help to determine the adhesive specificities of animal cells. Crystal-structure determination of ectodomain regions from three type II cadherins reveals adhesive dimers formed by exchange of N-terminal beta strands between partner extracellular cadherin-1 (EC1) domains. These interfaces have two conserved tryptophan side chains that anchor each swapped strand, compared with one in type I cadherins, and include large hydrophobic regions unique to type II interfaces. The EC1 domains of type I and type II cadherins appear to encode cell adhesive specificity in vitro. Moreover, perturbation of motor neuron segregation with chimeric cadherins depends on EC1 domain identity, suggesting that this region, which includes the structurally defined adhesive interface, encodes type II cadherin functional specificity in vivo.


==Overview==
Type II cadherin ectodomain structures: implications for classical cadherin specificity.,Patel SD, Ciatto C, Chen CP, Bahna F, Rajebhosale M, Arkus N, Schieren I, Jessell TM, Honig B, Price SR, Shapiro L Cell. 2006 Mar 24;124(6):1255-68. PMID:16564015<ref>PMID:16564015</ref>
Type I and II classical cadherins help to determine the adhesive specificities of animal cells. Crystal-structure determination of ectodomain regions from three type II cadherins reveals adhesive dimers formed by exchange of N-terminal beta strands between partner extracellular cadherin-1 (EC1) domains. These interfaces have two conserved tryptophan side chains that anchor each swapped strand, compared with one in type I cadherins, and include large hydrophobic regions unique to type II interfaces. The EC1 domains of type I and type II cadherins appear to encode cell adhesive specificity in vitro. Moreover, perturbation of motor neuron segregation with chimeric cadherins depends on EC1 domain identity, suggesting that this region, which includes the structurally defined adhesive interface, encodes type II cadherin functional specificity in vivo.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2A4C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A4C OCA].
</div>
<div class="pdbe-citations 2a4c" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Type II cadherin ectodomain structures: implications for classical cadherin specificity., Patel SD, Ciatto C, Chen CP, Bahna F, Rajebhosale M, Arkus N, Schieren I, Jessell TM, Honig B, Price SR, Shapiro L, Cell. 2006 Mar 24;124(6):1255-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16564015 16564015]
*[[Cadherin|Cadherin]]
*[[Cadherin 3D structures|Cadherin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Bahna F]]
[[Category: Bahna, F.]]
[[Category: Chen CP]]
[[Category: Chen, C P.]]
[[Category: Ciatto C]]
[[Category: Ciatto, C.]]
[[Category: Honig B]]
[[Category: Honig, B.]]
[[Category: Jessell TM]]
[[Category: Jessell, T M.]]
[[Category: Patel SD]]
[[Category: Patel, S D.]]
[[Category: Price SR]]
[[Category: Price, S R.]]
[[Category: Rajebhosale M]]
[[Category: Rajebhosale, M.]]
[[Category: Schieren I]]
[[Category: Schieren, I.]]
[[Category: Shapiro L]]
[[Category: Shapiro, L.]]
[[Category: Cadherin]]
[[Category: Dimer]]
[[Category: Extracellular domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:35:01 2008''
Retrieved from "https://proteopedia.org/2a4c"