Type II Cadherin Ectodomain Structures: Implications for Classical Cadherin Specificity
Copyright policy )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 beta 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.
- King’s University United States
- University College London United Kingdom
- Columbia University United States
- Howard Hughes Medical Institute United States
Models, Molecular, Binding Sites, Biochemistry, Genetics and Molecular Biology(all), Surface Properties, Xenopus Proteins, Cadherins, Crystallography, X-Ray, Cell Line, Protein Structure, Tertiary, Mice, Animals, Humans, Amino Acid Sequence, Chickens, Dimerization, Sequence Alignment, Cells, Cultured, Protein Binding
Models, Molecular, Binding Sites, Biochemistry, Genetics and Molecular Biology(all), Surface Properties, Xenopus Proteins, Cadherins, Crystallography, X-Ray, Cell Line, Protein Structure, Tertiary, Mice, Animals, Humans, Amino Acid Sequence, Chickens, Dimerization, Sequence Alignment, Cells, Cultured, Protein Binding
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