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Type II Cadherin Ectodomain Structures: Implications for Classical Cadherin Specificity

Type I and II classical cadherins help to determine the adhesive specificities of animal cells. Crystal-structure determination of ectodomain regions from three type II cadherins reveals adhesive dimers formed by exchange of N-terminal β strands between partner extracellular cadherin-1 (EC1) domains...

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Bibliographic Details
Published in:Cell 2006-03, Vol.124 (6), p.1255-1268
Main Authors: Patel, Saurabh D., Ciatto, Carlo, Chen, Chien Peter, Bahna, Fabiana, Rajebhosale, Manisha, Arkus, Natalie, Schieren, Ira, Jessell, Thomas M., Honig, Barry, Price, Stephen R., Shapiro, Lawrence
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Language:English
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Summary:Type I and II classical cadherins help to determine the adhesive specificities of animal cells. Crystal-structure determination of ectodomain regions from three type II cadherins reveals adhesive dimers formed by exchange of N-terminal β strands between partner extracellular cadherin-1 (EC1) domains. These interfaces have two conserved tryptophan side chains that anchor each swapped strand, compared with one in type I cadherins, and include large hydrophobic regions unique to type II interfaces. The EC1 domains of type I and type II cadherins appear to encode cell adhesive specificity in vitro. Moreover, perturbation of motor neuron segregation with chimeric cadherins depends on EC1 domain identity, suggesting that this region, which includes the structurally defined adhesive interface, encodes type II cadherin functional specificity in vivo.
ISSN:0092-8674
1097-4172
DOI:10.1016/j.cell.2005.12.046