Cadherin
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- | <StructureSection load='2a4c' size=' | + | <StructureSection load='2a4c' size='350' side='right' scene='41/417481/Cv/4' caption='Mouse cadherin-11 EC1 dimer (PDB code [[2a4c]])'> |
- | + | __TOC__ | |
== 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 /> |
- | *'''Desmogleins''' (Des-CDH) are CDH found in desmosomes. | + | *'''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) and '''desmocollin''' are CDH found in desmosomes. | ||
+ | |||
== Structural highlights == | == 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 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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== 3D Structures of Cadherin == | == 3D Structures of Cadherin == | ||
+ | [[Cadherin 3D structures]] | ||
- | + | </StructureSection> | |
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- | **[[2yqg]] – hDes-CDH EC1<br /> | ||
- | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
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References
- ↑ 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