Cadherin: Difference between revisions
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== Function == | == Function == | ||
[[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 /> | [[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 /> *'''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 /> | ||
*'''Desmogleins''' (Des-CDH) are CDH found in desmosomes. | *'''Desmogleins''' (Des-CDH) are CDH found in desmosomes. | ||
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**[[1zxk]] – mCDH8 EC1<br /> | **[[1zxk]] – mCDH8 EC1<br /> | ||
**[[2a62]] - mCDH8 EC1 | **[[2a62]] - mCDH8 EC1-EC3<br /> | ||
* CDH11 | * CDH11 | ||
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**[[2wbx]] – mCDH23 EC1<br /> | **[[2wbx]] – mCDH23 EC1<br /> | ||
**[[2wcp]] - mCDH23 EC2<br /> | **[[2wcp]] - mCDH23 EC2<br /> | ||
**[[2wd0]] - mCDH23 EC1 | **[[2wd0]] - mCDH23 EC1-EC2 (mutant)<br /> | ||
**[[4apx]], [[4aq8]], [[4axw]], [[4xxw]] - mCDH23 EC1 | **[[5tfm]] - mCDH23 EC6-EC8<br /> | ||
**[[4aqa]], [[4aqe]] - mCDH23 EC1 | **[[5tfl]] - mCDH23 EC7-EC8<br /> | ||
**[[5tfk]] - mCDH23 EC19-EC21<br /> | |||
**[[5i8d]], [[5ulu]], [[5un2]] - mCDH23 EC19-EC21 (mutant)<br /> | |||
**[[5uz8]] - mCDH23 EC22-EC24<br /> | |||
**[[4apx]], [[4aq8]], [[4axw]], [[4xxw]] - mCDH23 EC1-EC2 + Prot-CDH15<br /> | |||
**[[4aqa]], [[4aqe]] - mCDH23 EC1-EC2 (mutant) + Prot-CDH15 | |||
* C-CDH “classical” | * C-CDH “classical” | ||
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* E-CDH epithelial or CDH1 | * E-CDH epithelial or CDH1 | ||
**[[1q1p]], [[1ff5]], [[1edh]], [[3lne]], [[3lnf]], [[3lng]], [[3lnh]], [[3lni]], [[2qvf]] – mE-CDH EC1 | **[[1q1p]], [[1ff5]], [[1edh]], [[3lne]], [[3lnf]], [[3lng]], [[3lnh]], [[3lni]], [[2qvf]] – mE-CDH EC1-EC2<br /> | ||
**[[3q2v]] – mE-CDH ectodomain<br /> | **[[3q2v]] – mE-CDH ectodomain<br /> | ||
**[[4zt1]], [[2o72]] – hE-CDH EC1+ | **[[4zt1]], [[2o72]] – hE-CDH EC1-EC2<br /> | ||
**[[1edh]] - mE-CDH EC1 | **[[4zte]] – hE-CDH EC1-EC2 + inhibitor<br /> | ||
**[[3q2l]], [[3q2n]], [[3qrb]] - mE-CDH EC1 | **[[1edh]] - mE-CDH EC1-EC2+Ca<br /> | ||
**[[3q2l]], [[3q2n]], [[3qrb]] - mE-CDH EC1-EC2 (mutant)<br /> | |||
**[[1suh]] – mE-CDH N-terminal - NMR<br /> | **[[1suh]] – mE-CDH N-terminal - NMR<br /> | ||
**[[1i7x]], [[1i7w]] – mE-CDH cytoplasmic domain +catenin<br /> | **[[1i7x]], [[1i7w]] – mE-CDH cytoplasmic domain +catenin<br /> | ||
**[[4qd2]] – mE-CDH + botulinum neurotoxin<br /> | **[[4qd2]] – mE-CDH + botulinum neurotoxin<br /> | ||
**[[3ifq]] – hE-CDH EC1 | **[[3ifq]] – hE-CDH EC1-EC3 <br /> | ||
**[[3ff7]], [[3ff8]] - hE-CDH EC1 | **[[3ff7]], [[3ff8]] - hE-CDH EC1-EC3+NK cell receptor<br /> | ||
**[[2omt]], [[2omu]], [[2omx]], [[2omz]], [[2omv]], [[2omw]], [[2omy]] – hE-CDH EC1+internalin (mutant)<br /> | **[[2omt]], [[2omu]], [[2omx]], [[2omz]], [[2omv]], [[2omw]], [[2omy]] – hE-CDH EC1+internalin (mutant)<br /> | ||
**[[1o6s]] – E-CDH N-terminal+internalin – ''Listeria monocytogenes''<br /> | **[[1o6s]] – E-CDH N-terminal+internalin – ''Listeria monocytogenes''<br /> | ||
**[[4qd2]] – mE-CDH + botulinum neurotoxin<br /> | **[[4qd2]] – mE-CDH + botulinum neurotoxin<br /> | ||
*K-CDH kidney or CDH6 | |||
**[[5veb]] – hK-CDH EC5 + antibody<br /> | |||
* T-CDH membrane bound | * T-CDH membrane bound | ||
**[[3k5r]] – mT-CDH EC1 | **[[3k5r]] – mT-CDH EC1-EC2<br /> | ||
**[[3k5s]] - cT-CDH EC1 | **[[3k5s]] - cT-CDH EC1-EC2 <br /> | ||
**[[3k6d]] - XlT-CDH EC1 <br /> | **[[3k6d]] - XlT-CDH EC1 <br /> | ||
**[[3k6f]] - mT-CDH EC1<br /> | **[[3k6f]] - mT-CDH EC1<br /> | ||
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**[[1op4]] - mN-CDH prodomain - NMR<br /> | **[[1op4]] - mN-CDH prodomain - NMR<br /> | ||
**[[3ubf]] – DmN-CDH ectodomain – ''Drosophila melanogaster''<br /> | **[[3ubf]] – DmN-CDH ectodomain – ''Drosophila melanogaster''<br /> | ||
**[[3ubh]] - DmN-CDH EC1- | **[[3ubh]] - DmN-CDH EC1-EC4<br /> | ||
**[[3ubg]] - DmN-CDH EC1- | **[[3ubg]] - DmN-CDH EC1-EC3 | ||
*P-CDH placental or CDH3 | *P-CDH placental or CDH3 | ||
**[[4nqq]] – mP-CDH EC1 | **[[4nqq]] – mP-CDH EC1-EC2<br /> | ||
**[[4oy9]], [[4zml]], [[4zmn]], [[4zmq]], [[4zmt]], [[4zmw]], [[4zmz]] – hP-CDH EC1 | **[[4oy9]], [[4zml]], [[4zmn]], [[4zmq]], [[4zmt]], [[4zmw]], [[4zmz]] – hP-CDH EC1-EC2<br /> | ||
**[[4zmo]], [[4zmp]], [[4zmv]], [[4zmx]], [[4zmy]] – hP-CDH EC1 | **[[4zmo]], [[4zmp]], [[4zmv]], [[4zmx]], [[4zmy]] – hP-CDH EC1-EC2 (mutant)<br /> | ||
**[[5jyl]], [[5jym]] – hP-CDH EC1 | **[[5jyl]], [[5jym]] – hP-CDH EC1-EC2 + SCFV TSP7<br /> | ||
*VE-CDH vascular epithelial | *VE-CDH vascular epithelial |
Revision as of 09:41, 4 April 2018
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:
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 04-April-2018
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