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
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Cell. 2006 Mar 24;124(6):1255-68. doi: 10.1016/j.cell.2005.12.046.
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.
I型和II型经典钙黏蛋白有助于确定动物细胞的黏附特异性。对三种II型钙黏蛋白胞外结构域区域的晶体结构测定揭示了由伙伴细胞外钙黏蛋白-1（EC1）结构域之间N端β链交换形成的黏附二聚体。与I型钙黏蛋白中的一个相比，这些界面有两个保守的色氨酸侧链来锚定每条交换的链，并且包括II型界面特有的大疏水区域。I型和II型钙黏蛋白的EC1结构域似乎在体外编码细胞黏附特异性。此外，嵌合钙黏蛋白对运动神经元分离的干扰取决于EC1结构域的特性，这表明这个包括结构上确定的黏附界面的区域在体内编码II型钙黏蛋白的功能特异性。
