2a62: Difference between revisions

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[[Image:2a62.gif|left|200px]]


{{Structure
==Crystal structure of mouse cadherin-8 EC1-3==
|PDB= 2a62 |SIZE=350|CAPTION= <scene name='initialview01'>2a62</scene>, resolution 4.50&Aring;
<StructureSection load='2a62' size='340' side='right'caption='[[2a62]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
<table><tr><td colspan='2'>[[2a62]] 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=2A62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A62 FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.5&#8491;</td></tr>
|GENE= Cdh8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<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>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a62 OCA], [https://pdbe.org/2a62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a62 RCSB], [https://www.ebi.ac.uk/pdbsum/2a62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a62 ProSAT]</span></td></tr>
|RELATEDENTRY=[[1zvn|1ZVN]], [[1zxk|1ZXK]], [[2a4c|2A4C]], [[2a4e|2A4E]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a62 OCA], [http://www.ebi.ac.uk/pdbsum/2a62 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a62 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CADH8_MOUSE CADH8_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/a6/2a62_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=2a62 ConSurf].
<div style="clear:both"></div>


'''Crystal structure of mouse cadherin-8 EC1-3'''
==See Also==
 
*[[Cadherin 3D structures|Cadherin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
2A62 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=2A62 OCA].
 
==Reference==
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]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Arkus N]]
[[Category: Arkus, N.]]
[[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: Schieren I]]
[[Category: Schieren, I.]]
[[Category: Shapiro L]]
[[Category: Shapiro, L.]]
[[Category: cadherin]]
[[Category: calcium binding]]
[[Category: extracellular domain]]
[[Category: homodimer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:48:18 2008''

Latest revision as of 12:11, 14 February 2024

Crystal structure of mouse cadherin-8 EC1-3Crystal structure of mouse cadherin-8 EC1-3

Structural highlights

2a62 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CADH8_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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2a62, resolution 4.50Å

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