Cadherin

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== Structural highlights ==
== 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/3'>2 Trp residues</scene> docking into the hydrophobic pocket of the neighboring CDH molecule.
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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/3'>2 Trp residues</scene> docking into the hydrophobic pocket of the neighboring CDH molecule. <ref>PMID:16564015</ref>
</StructureSection>
</StructureSection>
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**[[2yqg]] – hDes-CDH EC1<br />
**[[2yqg]] – hDes-CDH EC1<br />
}}
}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 13:20, 17 November 2015

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

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3D Structures of Cadherin

Updated on 17-November-2015

References

  1. 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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Michal Harel, Alexander Berchansky

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