Overduin M, Harvey T S, Bagby S, Tong K I, Yau P, Takeichi M, Ikura M
Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.
Science. 1995 Jan 20;267(5196):386-9. doi: 10.1126/science.7824937.
Cadherins are calcium-dependent cell adhesion molecules containing extracellular repeats of approximately 110 amino acids. The three-dimensional structure of the amino-terminal repeat of mouse epithelial cadherin was determined by multidimensional heteronuclear magnetic resonance spectroscopy. The calcium ion was bound by a short alpha helix and by loops at one end of the seven-stranded beta-barrel structure. An exposed concave face is in a position to provide homophilic binding specificity and was also sensitive to calcium ligation. Unexpected structural similarities with the immunoglobulin fold suggest an evolutionary relation between calcium-dependent and calcium-independent cell adhesion molecules.
钙黏着蛋白是一类依赖于钙的细胞黏附分子，含有约110个氨基酸的细胞外重复序列。通过多维异核磁共振波谱法确定了小鼠上皮钙黏着蛋白氨基末端重复序列的三维结构。钙离子由一个短α螺旋和七链β桶状结构一端的环所结合。一个暴露的凹面能够提供嗜同性结合特异性，并且对钙连接也很敏感。与免疫球蛋白折叠意外的结构相似性表明了依赖钙和不依赖钙的细胞黏附分子之间的进化关系。
