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Cadherin

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<StructureSection load='2a4c' size='350' side='right' scene='41/417481/Cv/2' caption='Mouse cadherin-11 EC1 dimer (PDB code [[2a4c]])'>
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<StructureSection load='2a4c' size='350' side='right' scene='41/417481/Cv/4' caption='Mouse cadherin-11 EC1 dimer (PDB code [[2a4c]])'>
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__TOC__
== Function ==
== Function ==
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[[Cadherin|Cadherins]] (CDH) are calcium-dependent adhesion proteins. They contain extracellular CDH repeats (EC1-EC5) which bind calcium ions. They are encoded by numerous genes numbered CDH1-CDH23. Some names of CDH indicate their locations: '''E-CDH''' (epithelial tissue), '''VE-CDH''' (vascular epithelial), '''T-CDH''' bound to membrane, '''N-CDH''' (neurons), '''P-CDH''' (placental). The CDH superfamily contains:<br /> *'''Protocadhedrins''' (Prot-CDH) which are similar to CDH but are unique in their cytoplasmic domains. They are found mainly in the brain at cell-cell contacts.<ref>PMID:11171368</ref> <br />
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[[Cadherin|Cadherins]] (CDH) are calcium-dependent adhesion proteins. They contain extracellular CDH repeats (EC1-EC5) which bind calcium ions. They are encoded by numerous genes numbered CDH1-CDH23. Some names of CDH indicate their locations: '''E-CDH''' (epithelial tissue), '''VE-CDH''' (vascular epithelial), '''T-CDH''' bound to membrane, '''N-CDH''' (neurons), '''P-CDH''' (placental), '''K-CDH''' (kidney). The CDH superfamily contains:<br />
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*'''Desmogleins''' (Des-CDH) are CDH found in desmosomes.
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*'''Protocadhedrins''' (Prot-CDH) which are similar to CDH but are unique in their cytoplasmic domains. They are found mainly in the brain at cell-cell contacts.<ref>PMID:11171368</ref> <br />
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*'''Desmogleins''' (Des-CDH) and '''desmocollin''' are CDH found in desmosomes.
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== Structural highlights ==
== Structural highlights ==
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The adhesive binding of CDH arises from the exchange of β strand of one CDH with the strand of CDH of a neighboring cell termed ''strand swap''. The strand swapping is enhanced by <scene name='41/417481/Cv/3'>2 Trp residues</scene> docking into the hydrophobic pocket of the neighboring CDH molecule. <ref>PMID:16564015</ref>
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The adhesive binding of CDH arises from the exchange of β strand of one CDH with the strand of CDH of a neighboring cell termed ''strand swap''. The strand swapping is enhanced by <scene name='41/417481/Cv/5'>2 Trp residues</scene> docking into the hydrophobic pocket of the neighboring CDH molecule. <ref>PMID:16564015</ref>
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</StructureSection>
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== 3D Structures of Cadherin ==
== 3D Structures of Cadherin ==
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[[Cadherin 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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* CDH5
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**[[2koh]] – mCDH5+PAR3-PDZ3 - mouse<br />
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* CDH6
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**[[3lnd]] – mCDH6 EC12 (mutant)<br />
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* CDH8
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**[[1zxk]] – mCDH8 EC1<br />
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**[[2a62]] - mCDH8 EC1+EC2+EC3<br />
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* CDH11
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**[[2a4c]], [[2a4e]] – mCDH11 EC1<br />
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* CDH20
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**[[1zvn]] – cCDH20 EC1 – chicken<br />
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* CDH23
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**[[3mvs]], [[2whv]] – mCDH23 N-terminal<br />
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**[[2kbr]] – hCDH23 peptide+harmonin – NMR - human<br />
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**[[2kbs]] - hCDH23 C-terminal peptide+harmonin PDZ2 – NMR<br />
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**[[2wbx]] – mCDH23 EC1<br />
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**[[2wcp]] - mCDH23 EC2<br />
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**[[2wd0]] - mCDH23 EC1+EC2 (mutant)<br />
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**[[4apx]], [[4aq8]], [[4axw]], [[4xxw]] - mCDH23 EC1+EC2 + Prot-CDH15<br />
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**[[4aqa]], [[4aqe]] - mCDH23 EC1+EC2 (mutant) + Prot-CDH15
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* C-CDH “classical”
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**[[1l3w]] – XlC-CDH ectodomain - ''Xenopus laevis''<br />
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**[[1q5b]], [[1q5c]], [[1q55]], [[1q5a]] – C-CDH model into desmosome – electron tomography<br />
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* E-CDH epithelial or CDH1
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**[[1q1p]], [[1ff5]], [[1edh]], [[3lne]], [[3lnf]], [[3lng]], [[3lnh]], [[3lni]], [[2qvf]] – mE-CDH EC1+EC2<br />
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**[[3q2v]] – mE-CDH ectodomain<br />
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**[[4zt1]], [[2o72]] – hE-CDH EC1+EC2<br />
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**[[1edh]] - mE-CDH EC1+EC2+Ca<br />
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**[[3q2l]], [[3q2n]], [[3qrb]] - mE-CDH EC1+EC2 (mutant)<br />
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**[[1suh]] – mE-CDH N-terminal - NMR<br />
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**[[1i7x]], [[1i7w]] – mE-CDH cytoplasmic domain +catenin<br />
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**[[4qd2]] – mE-CDH + botulinum neurotoxin<br />
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**[[3ifq]] – hE-CDH EC1+EC2+EC3 <br />
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**[[3ff7]], [[3ff8]] - hE-CDH EC1+EC2+EC3+NK cell receptor<br />
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**[[2omt]], [[2omu]], [[2omx]], [[2omz]], [[2omv]], [[2omw]], [[2omy]] – hE-CDH EC1+internalin (mutant)<br />
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**[[1o6s]] – E-CDH N-terminal+internalin – ''Listeria monocytogenes''<br />
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**[[4qd2]] – mE-CDH + botulinum neurotoxin<br />
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* T-CDH membrane bound
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**[[3k5r]] – mT-CDH EC1+EC2<br />
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**[[3k5s]] - cT-CDH EC1+EC2 <br />
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**[[3k6d]] - XlT-CDH EC1 <br />
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**[[3k6f]] - mT-CDH EC1<br />
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**[[3k6i]] - cT-CDH EC1<br />
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**[[2v37]] – hT-CDH N-terminal - NMR<br />
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* N-CDH neuronal
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**[[1nch]], [[1nci]] – mN-CDH<br />
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**[[1ncg]] – mN-CDH (mutant)<br />
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**[[2qvi]], [[4nuq]] – mN-CDH EC1-EC2<br />
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**[[4num]], [[4nup]] – mN-CDH EC1-EC2 (mutant)<br />
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**[[1ncj]] – mN-CDH two domains<br />
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**[[3q2w]] – mN-CDH ectodomain<br />
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**[[1op4]] - mN-CDH prodomain - NMR<br />
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**[[3ubf]] – DmN-CDH ectodomain – ''Drosophila melanogaster''<br />
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**[[3ubh]] - DmN-CDH EC1-4<br />
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**[[3ubg]] - DmN-CDH EC1-3
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*P-CDH placental or CDH3
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**[[4nqq]] – mP-CDH EC1+EC2<br />
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**[[4oy9]], [[4zml]], [[4zmn]], [[4zmq]], [[4zmt]], [[4zmw]], [[4zmz]] – hP-CDH EC1+EC2<br />
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**[[4zmo]], [[4zmp]], [[4zmv]], [[4zmx]], [[4zmy]] – hP-CDH EC1+EC2 (mutant)<br />
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**[[5jyl]], [[5jym]] – hP-CDH EC1+EC2 + SCFV TSP7<br />
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*VE-CDH vascular epithelial
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**[[3ppe]] – cVE-CDH EC1+EC2<br />
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* Protocadherin
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**[[2yst]] – hProt-CDH7 EC3 – NMR<br />
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**[[2ee0]] - hProt-CDH9 Ca domain – NMR<br />
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**[[1wyj]] - mProt-CDH β 14 - NMR<br />
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**[[1wuz]] - mProt-CDH4 EC1 – NMR<br />
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**[[5cyx]] - mProt-CDH2 EC1+EC2+EC3<br />
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* Desmoglein
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**[[2yqg]] – hDes-CDH2 EC1<br />
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**[[5erd]] – hDes-CDH2 ectodomain<br />
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**[[5eqx]] – hDes-CDH3 ectodomain<br />
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*Desmocollin
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**[[5iry]] – hDesmc1 ectodomain<br />
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**[[5erp]], [[5j5j]] – hDesmc2 ectodomain<br />
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Mouse cadherin-11 EC1 dimer (PDB code 2a4c)

Drag the structure with the mouse to rotate

References

  1. ↑ Angst BD, Marcozzi C, Magee AI. The cadherin superfamily: diversity in form and function. J Cell Sci. 2001 Feb;114(Pt 4):629-41. PMID:11171368
  2. ↑ Patel SD, Ciatto C, Chen CP, Bahna F, Rajebhosale M, Arkus N, Schieren I, Jessell TM, Honig B, Price SR, Shapiro L. Type II cadherin ectodomain structures: implications for classical cadherin specificity. Cell. 2006 Mar 24;124(6):1255-68. PMID:16564015 doi:http://dx.doi.org/10.1016/j.cell.2005.12.046

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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