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Cadherin

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(New page: Crystal Structure of Cadherin, 1q1p {{STRUCTURE_1q1p| PDB=1q1p | SIZE=300| SCENE= |right|CAPTION=Cadherin, 1q1p }} '''Cadherins''' (CDH) are ...)
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[[Image:1q1p.png|left|200px|thumb|Crystal Structure of Cadherin, [[1q1p]]]]
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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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{{STRUCTURE_1q1p| PDB=1q1p | SIZE=300| SCENE= |right|CAPTION=Cadherin, [[1q1p]] }}
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__TOC__
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== Function ==
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'''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), T-CDH bound to membrane, N-CDH (neurons). The CDH superfamily contains protocadhedrins (Prot-CDH), desmogleins (Des-CDH) and more. The images at the left and at the right correspond to one representative Cadherin, ''i.e.'' the crystal structure of Cadherin ([[1q1p]]). Calcium ions is shown as a space filling objects.
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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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*'''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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{{TOC limit|limit=2}}
 
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== 3D Structures of Cadherin ==
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== 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/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 ==
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[[Cadherin 3D structures]]
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CDH encoded by CDH1
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</StructureSection>
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1q1p – mCDH1 - mouse
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CDH encoded by CDH5
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2koh – mCDH5+PAR3-PDZ3
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CDH encoded by CDH6
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3lnd – mCDH6 EC12 (mutant)
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CDH encoded by CDH8
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1zxk – mCDH8 EC1
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2a62 - mCDH8 EC1+EC2+EC3
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CDH encoded by CDH11
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2a4c, 2a4e – mCDH11 EC1
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CDH encoded by CDH20
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1zvn – cCDH20 EC1 – chicken
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CDH encoded by CDH23
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3mvs, 2whv – mCDH23 N-terminal
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2kbr – hCDH23 peptide+harmonin – NMR - human
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2kbs - hCDH23 C-terminal peptide+harmonin PDZ2 – NMR
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C-CDH “classical”
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1l3w – XlC-CDH ectodomain - Xenopus laevis
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1q5b, 1q5c – C-CDH model into desmosome – electron tomography
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E-CDH epithelial
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1ff5 – mE-CDH double domain
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1edh - mE-CDH EC1+EC2+Ca
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1suh – mE-CDH N-terminal - NMR
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3l6x, 3l6y, 1i7x, 1i7w – mE-CDH+catenin
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3lne, 3lnf, 3lng, 3lnh, 3lni – mE-CDH EC12 (mutant)
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3ifq – hE-CDH EC1+EC2+EC3
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2o72 - hE-CDH EC1+EC2
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3ff7, 3ff8 - hE-CDH EC1+EC2+EC3+NK cell receptor
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2qvf – mE-CDH1 CDH2
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2omt, 2omu, 2omx, 2omz, 2omv, 2omw, 2omy – hE-CDH EC1+internalin (mutant)
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1o6s – E-CDH N-terminal+internalin – Listeria monocytogenes
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T-CDH membrane bound
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3k5r – mT-CDH EC1+EC2
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3k5s - cT-CDH EC1+EC2
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3k6d - XlT-CDH EC1
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3k6f - mT-CDH EC1
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3k6i - cT-CDH EC1
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2v37 – hT-CDH N-terminal - NMR
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N-CDH neuronal
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1nch, 1nci – mN-CDH
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1ncg – mN-CDH (mutant)
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2qvi – mN-CDH EC12
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1ncj – mN-CDH two domains
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Protocadherin
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2yst – hProt-CDH7 EC3 – NMR
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Desmoglein
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2yqg – hDes-CDH EC1
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== References ==
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<references/>
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[[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

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