FunctionCadherins (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 highlightsThe 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]
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3D Structures of Cadherin3D Structures of Cadherin
Updated on 08-January-2019
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- CDH5
- 2koh – mCDH5+PAR3-PDZ3 - mouse
- CDH6
- 3lnd – mCDH6 EC12 (mutant)
- CDH8
- CDH11
- CDH20
- 1zvn – cCDH20 EC1 – chicken
- CDH23
- 3mvs, 2whv – mCDH23 N-terminal
- 2kbr – hCDH23 peptide+harmonin – NMR - human
- 2kbs - hCDH23 C-terminal peptide+harmonin PDZ2 – NMR
- 2wbx – mCDH23 EC1
- 2wcp - mCDH23 EC2
- 2wd0 - mCDH23 EC1-EC2 (mutant)
- 5tfm - mCDH23 EC6-EC8
- 5tfl - mCDH23 EC7-EC8
- 5tfk - mCDH23 EC19-EC21
- 5i8d, 5ulu, 5un2 - mCDH23 EC19-EC21 (mutant)
- 5uz8 - mCDH23 EC22-EC24
- 4apx, 4aq8, 4axw, 4xxw - mCDH23 EC1-EC2 + Prot-CDH15
- 4aqa, 4aqe - mCDH23 EC1-EC2 (mutant) + Prot-CDH15
- C-CDH “classical”
- 1l3w – XlC-CDH ectodomain - Xenopus laevis
- 1q5b, 1q5c, 1q55, 1q5a – C-CDH model into desmosome – electron tomography
- E-CDH epithelial or CDH1
- 1q1p, 1ff5, 1edh, 3lne, 3lnf, 3lng, 3lnh, 3lni, 2qvf – mE-CDH EC1-EC2
- 3q2v – mE-CDH ectodomain
- 4zt1, 2o72 – hE-CDH EC1-EC2
- 4zte – hE-CDH EC1-EC2 + inhibitor
- 1edh - mE-CDH EC1-EC2+Ca
- 3q2l, 3q2n, 3qrb - mE-CDH EC1-EC2 (mutant)
- 1suh – mE-CDH N-terminal - NMR
- 1i7x, 1i7w – mE-CDH cytoplasmic domain +catenin
- 4qd2 – mE-CDH + botulinum neurotoxin
- 3ifq – hE-CDH EC1-EC3
- 3ff7, 3ff8 - hE-CDH EC1-EC3+NK cell receptor
- 2omt, 2omu, 2omx, 2omz, 2omv, 2omw, 2omy – hE-CDH EC1+internalin (mutant)
- 1o6s – E-CDH N-terminal+internalin – Listeria monocytogenes
- 4qd2 – mE-CDH + botulinum neurotoxin
- K-CDH kidney or CDH6
- 5veb – hK-CDH EC5 + antibody
- T-CDH membrane bound
- 3k5r – mT-CDH EC1-EC2
- 3k5s - cT-CDH EC1-EC2
- 3k6d - XlT-CDH EC1
- 3k6f - mT-CDH EC1
- 3k6i - cT-CDH EC1
- 2v37 – hT-CDH N-terminal - NMR
- N-CDH neuronal
- 1nch, 1nci – mN-CDH
- 1ncg – mN-CDH (mutant)
- 2qvi, 4nuq – mN-CDH EC1-EC2
- 4num, 4nup – mN-CDH EC1-EC2 (mutant)
- 1ncj – mN-CDH two domains
- 3q2w – mN-CDH ectodomain
- 1op4 - mN-CDH prodomain - NMR
- 3ubf – DmN-CDH ectodomain – Drosophila melanogaster
- 3ubh - DmN-CDH EC1-EC4
- 3ubg - DmN-CDH EC1-EC3
- P-CDH placental or CDH3
- 4nqq – mP-CDH EC1-EC2
- 4oy9, 4zml, 4zmn, 4zmq, 4zmt, 4zmw, 4zmz – hP-CDH EC1-EC2
- 4zmo, 4zmp, 4zmv, 4zmx, 4zmy – hP-CDH EC1-EC2 (mutant)
- 5jyl, 5jym – hP-CDH EC1-EC2 + SCFV TSP7
- VE-CDH vascular epithelial
- Protocadherin
- 2yst – hProt-CDH7 EC3 – NMR
- 2ee0 - hProt-CDH9 Ca domain – NMR
- 1wyj - mProt-CDH β 14 - NMR
- 1wuz - mProt-CDH4 EC1 – NMR
- 5cyx - mProt-CDH2 EC1+EC2+EC3
- Desmoglein
- 2yqg – hDes-CDH2 EC1
- 5erd – hDes-CDH2 ectodomain
- 5eqx – hDes-CDH3 ectodomain
- Desmocollin
ReferencesReferences
- ↑ 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
- ↑ 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