Olsen K W
Biochim Biophys Acta. 1983 Mar 16;743(2):212-8. doi: 10.1016/0167-4838(83)90216-9.
The circularly permuted sequence homology that relates concanavalin A to the other leguminous plant lectins can be explained by an evolutionary model that requires three exons. The identification of these potential exons from the amino acid sequence data allows the prediction of three domains in the lectin structure. The predicted domains are reasonable, functional and structural units in concanavalin A, demonstrating the correspondence of exons and domains. In addition, slight modifications to the three-dimensional structure of concanavalin A produced a model which was consistent with the sequence data for the other plant lectins.
伴刀豆球蛋白A与其他豆科植物凝集素相关的环状排列序列同源性可以用一个需要三个外显子的进化模型来解释。从氨基酸序列数据中识别出这些潜在的外显子，使得能够预测凝集素结构中的三个结构域。预测的结构域是伴刀豆球蛋白A中合理的、功能性和结构性单元，证明了外显子与结构域的对应关系。此外，对伴刀豆球蛋白A三维结构的轻微修改产生了一个与其他植物凝集素序列数据一致的模型。
