Brümmendorf T, Rathjen F G
Max-Planck-Institut für Entwicklungsbiologie,Tübingen, Germany.
Curr Opin Neurobiol. 1996 Oct;6(5):584-93. doi: 10.1016/s0959-4388(96)80089-4.
Evidence is accumulating that axonal members of the Ig superfamily (IgSF) interact in a complex manner with other axonal Ig-like proteins and with proteins of the extracellular matrix. Studies investigating the structure/function relationships of these proteins have highlighted the importance of Ig-like domains near the amino terminus (N-proximal) as both necessary and sufficient for homophilic and heterophilic binding. Although efforts have been made in the past year to correlate the structure and neurite-outgrowth-promoting ability of axonal IgSF members, this work is still at an early stage.
越来越多的证据表明,免疫球蛋白超家族(IgSF)的轴突成员与其他轴突免疫球蛋白样蛋白以及细胞外基质蛋白以复杂的方式相互作用。研究这些蛋白质结构/功能关系的研究突出了氨基末端附近(N近端)的免疫球蛋白样结构域对于同种亲和性和异种亲和性结合的必要性和充分性。尽管在过去一年中已经努力将轴突IgSF成员的结构与促进神经突生长的能力相关联,但这项工作仍处于早期阶段。