Potts J R, Campbell I D
Department of Biochemistry, University of Oxford, UK.
Curr Opin Cell Biol. 1994 Oct;6(5):648-55. doi: 10.1016/0955-0674(94)90090-6.
Significant progress has been made recently in the determination of the structure and assembly of the important matrix protein fibronectin, a molecule mainly constructed from three modular units denoted Fn1, Fn2 and Fn3. Atomic resolution structures are now available for all three single modules, for Fn1 and Fn3 module pairs, and for the disulphide-linked join between fibronectin monomers. Combined with results from new binding and mutation studies, the new structural information is leading to a clearer view of structure/function relationships in intact fibronectin.
近期,在重要的基质蛋白纤连蛋白的结构测定和组装方面取得了重大进展。纤连蛋白主要由三个模块化单元Fn1、Fn2和Fn3构成。目前,所有三个单一模块、Fn1和Fn3模块对以及纤连蛋白单体之间的二硫键连接的原子分辨率结构均已获得。结合新的结合和突变研究结果,这些新的结构信息使人们对完整纤连蛋白的结构/功能关系有了更清晰的认识。