By John Cosimano
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This suggests that residues 717-724 of the p3 cytoplasmic tail maintain allbp3 in a default low-affinity state. Puzon-McLaughlin and co-workers (1996) used the conformation-dependent and activation-specific anti-pl mAb 15/7 to show that truncation of more than 16 residues of the p l cytoplasmic domain resulted in a constitutively low-affinity state in agreement with the consensus that nearly all of the p cytoplasmic tail is required for integrin activation. A recent report by Baker et al. (1997) has confirmed the requirement for a near full length p l cytoplasmic domain.
1991). While clearly conserved, a comparison of the primary structure of the cadherin repeats reveals a clear divergence between repeats from the different cadherin groups, and even between one repeat and another within one protein. In contrast to the conservation of the extracellular structure of cadherins, which is the primary basis for the identification of a cadherin as such, the cytoplasmic domains show a much higher variability among the different cadherin classes. These differences may well reflect separate functions of the four cadherin classes.
43 45 A. Loss-of-Function Analysis . . . B. Dominant-Negative Approach . . . . . . . . . . . . . . . . . . . 4 6 Advances in Molecular and Cell Biology Volume 28, pages 27-63. Copyright 0 1999 by JAI Press Inc. All right of reproduction in any form reserved. ISBN: 0-7623-0495-2 27 28 JORG STAPPERT and ROLF KEMLER VI. The Cadherin-Catenin Complex in Signal Transduction andpathogenesis . . . . . . . . . . . . . . . . . . . . VII. Conclusions . .