Cadherin: Difference between revisions

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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>
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>
== 3D Structures of Cadherin ==
[[Cadherin 3D structures]]


</StructureSection>
</StructureSection>
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**[[3lnd]] – mCDH6 EC12 (mutant)<br />
**[[3lnd]] – mCDH6 EC12 (mutant)<br />
*CDH encoded by CDH7
**[[6cgs]] – mCDH7 EC1-EC2<br />


* CDH8  
* CDH8  
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**[[2a4c]], [[2a4e]] – mCDH11 EC1<br />
**[[2a4c]], [[2a4e]] – mCDH11 EC1<br />
**[[6cgb]] - mCDH11 EC1/CDH6 EC2<br />


* CDH20  
* CDH20  


**[[1zvn]] – cCDH20 EC1 – chicken<br />
**[[1zvn]] – cCDH20 EC1 – chicken<br />
*CDH encoded by CDH22
**[[6cg7]] – mCDH20 EC1-EC2<br />


* CDH23  
* CDH23  
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**[[2wcp]] - mCDH23 EC2<br />
**[[2wcp]] - mCDH23 EC2<br />
**[[2wd0]] - mCDH23 EC1-EC2 (mutant)<br />
**[[2wd0]] - mCDH23 EC1-EC2 (mutant)<br />
**[[5w4t]] - CDH23 EC1-EC3 - zebrafish<br />
**[[5tfm]] - mCDH23 EC6-EC8<br />
**[[5tfm]] - mCDH23 EC6-EC8<br />
**[[5tfl]] - mCDH23 EC7-EC8<br />
**[[5tfl]] - mCDH23 EC7-EC8<br />
**[[5vh2]] - mCDH23 EC12-EC13 (mutant)<br />
**[[5wj8]] - hCDH23 EC13-EC14<br />
**[[5wjm]] - mCDH23 EC17-EC18<br />
**[[5tfk]] - mCDH23 EC19-EC21<br />
**[[5tfk]] - mCDH23 EC19-EC21<br />
**[[5i8d]], [[5ulu]], [[5un2]] - mCDH23 EC19-EC21 (mutant)<br />
**[[5i8d]], [[5ulu]], [[5un2]] - mCDH23 EC19-EC21 (mutant)<br />
**[[5vvm]] - hCDH23 EC21-EC23<br />
**[[5uz8]] - mCDH23 EC22-EC24<br />
**[[5uz8]] - mCDH23 EC22-EC24<br />
**[[5vt8]] - mCDH23 EC23-EC25<br />
**[[4apx]], [[4aq8]], [[4axw]], [[4xxw]] - mCDH23 EC1-EC2 + Prot-CDH15<br />
**[[4apx]], [[4aq8]], [[4axw]], [[4xxw]] - mCDH23 EC1-EC2 + Prot-CDH15<br />
**[[4aqa]], [[4aqe]] - mCDH23 EC1-EC2 (mutant) + Prot-CDH15
**[[4aqa]], [[4aqe]] - mCDH23 EC1-EC2 (mutant) + Prot-CDH15
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**[[4zt1]], [[2o72]] – hE-CDH EC1-EC2<br />
**[[4zt1]], [[2o72]] – hE-CDH EC1-EC2<br />
**[[4zte]] – hE-CDH EC1-EC2 + inhibitor<br />
**[[4zte]] – hE-CDH EC1-EC2 + inhibitor<br />
**[[6fek]] – hE-CDH EC1-EC2 + antibody<br />
**[[1edh]] - mE-CDH EC1-EC2+Ca<br />
**[[1edh]] - mE-CDH EC1-EC2+Ca<br />
**[[3q2l]], [[3q2n]], [[3qrb]] - mE-CDH EC1-EC2 (mutant)<br />
**[[3q2l]], [[3q2n]], [[3qrb]] - mE-CDH EC1-EC2 (mutant)<br />
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**[[5veb]] – hK-CDH EC5 + antibody<br />
**[[5veb]] – hK-CDH EC5 + antibody<br />
**[[6cgu]] – mK-CDH EC1-EC2 <br />


* T-CDH membrane bound  
* T-CDH membrane bound  


**[[3k5r]] – mT-CDH EC1-EC2<br />
**[[3k5r]], [[6cg6]] – mT-CDH EC1-EC2<br />
**[[3k5s]] - cT-CDH EC1-EC2 <br />
**[[3k5s]] - cT-CDH EC1-EC2 <br />
**[[3k6d]] - XlT-CDH EC1 <br />
**[[3k6d]] - XlT-CDH EC1 <br />
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* Protocadherin  
* Protocadherin  


**[[6bx7]] - hProt-CDH1 EC1-EC4<br />
**[[2yst]] – hProt-CDH7 EC3 – NMR<br />
**[[2yst]] – hProt-CDH7 EC3 – NMR<br />
**[[2ee0]] - hProt-CDH9 Ca domain – NMR<br />
**[[2ee0]] - hProt-CDH9 Ca domain – NMR<br />
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**[[1wuz]] - mProt-CDH4 EC1 – NMR<br />
**[[1wuz]] - mProt-CDH4 EC1 – NMR<br />
**[[5cyx]] - mProt-CDH2 EC1+EC2+EC3<br />
**[[5cyx]] - mProt-CDH2 EC1+EC2+EC3<br />
**[[5szl]] - mProt-CDH γ A1 EC1-EC4<br />


* Desmoglein  
* Desmoglein  
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**[[5erd]] – hDes-CDH2 ectodomain<br />
**[[5erd]] – hDes-CDH2 ectodomain<br />
**[[5eqx]] – hDes-CDH3 ectodomain<br />
**[[5eqx]] – hDes-CDH3 ectodomain<br />
**[[6qnt]], [[6qnu]] – hDesmc2 ectodomain + adenovirus fiber protein – Cryo EM<br />


*Desmocollin
*Desmocollin

Revision as of 13:32, 18 April 2019


Function

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:
*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.[1]

  • Desmogleins (Des-CDH) are CDH found in desmosomes.

Structural highlights

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 docking into the hydrophobic pocket of the neighboring CDH molecule. [2]

3D Structures of Cadherin

Cadherin 3D structures


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

Drag the structure with the mouse to rotate

3D Structures of Cadherin3D Structures of Cadherin

Updated on 18-April-2019

ReferencesReferences

  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?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel