Calcium-binding epidermal growth factor

Cardy, C. M., and Handford, P. A. (1998). Metal ion dependency of microfibrils supports a rod-like conformation for fibrillin-1 calcium-binding epidermal growth factor-like domains. J. Mol. Biol. 276, 855-860. 

Reinhardt, D. P., Ono, R. N., Notbohm, H., Muller, P. K., Bachinger, H. P., and Sakai, L. Y. (2000a). Mutations in calcium-binding epidermal growth factor modules render fibrillin-1 susceptible to proteolysis. A potential disease-causing mechanism in Marfan syndrome. / Biol. Chem. 275, 12339-12345. 

Smallridge, R. S., Whiteman, P., Werner, J. M., Campbell, I. D., Handford, P. A., and Downing, A. K. (2003). Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1./. Biol. Chem. 278, 12199-12206. 

Figure 2.19 Organization of polypeptide chains into domains. Small protein molecules like the epidermal growth factor, EGF, comprise only one domain. Others, like the serine proteinase chymotrypsin, are arranged in two domains that are required to form a functional unit (see Chapter 11). Many of the proteins that are involved in blood coagulation and fibrinolysis, such as urokinase, factor IX, and plasminogen, have long polypeptide chains that comprise different combinations of domains homologous to EGF and serine proteinases and, in addition, calcium-binding domains and Kringle domains.

---