STRUCTURE OF THE FIBRONECTIN TYPE 1 MODULE

THE rapid accumulation of sequence data has provided insight into the evolution of proteins and led to the identification of 'mosaic proteins'1,2. These proteins have evolved by duplication, insertion and deletion of a common pool of structural units or modules, yet their biological functions are diverse. They are involved in cell adhesion and migration3, embryogenesis4 and the pathways of blood clotting, fibrinolysis and complement5,6. The modular units are defined by 'consensus sequences' which often include conserved disulphide bonds. Despite the available sequence information, little is known of the tertiary structure of mosaic proteins. If, however, the 'consensus structure' of the modules were known, valuable structural information could be inferred about a wide variety of proteins and biological systems. An important mosaic protein is fibronectin, an extracellular matrix protein that consists of three types of module (see refs 3,7 for reviews). Here we describe the structure of the fibronectin type 1 module which appears twelve times in fibronectin and is also found in factor XII8 and tissue plasminogen activator9. The module was produced using a yeast expression system and the structure was determined in solution using 1H NMR. This methodology promises to be extremely powerful in the investigation of modules from a wide range of mosaic proteins. © 1990 Nature Publishing Group.