In molecular biology, the CFC domain (Cripto_Frl-1_Cryptic domain) is a protein domain found at the C-terminus of a number of proteins including Cripto (or teratocarcinoma-derived growth factor).[1][2] It is structurally similar to the C-terminal extracellular portions of Jagged 1 and Jagged 2.[1] CFC is approx 40-residues long, compacted by three internal disulphide bridges, and bindsAlk4 via a hydrophobic patch. CFC is structurally homologous to the VWFC-like domain.[1]
The CFC domain appears to play a crucial role in the tumourigenic activity of Cripto proteins, as it is through the CFC domain that Cripto interferes with the onco-suppressive activity of Activins, either by blocking the Activin receptor ALK4 or by antagonising proteins of the TGF-beta family.[3]
^Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M (November 2006). "Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala". J. Med. Chem. 49 (24): 7054–62. doi:10.1021/jm060772r. PMID17125258.
^Calvanese L, Saporito A, Oliva R, D' Auria G, Pedone C, Paolillo L, Ruvo M, Marasco D, Falcigno L (March 2009). "Structural insights into the interaction between the Cripto CFC domain and the ALK4 receptor". J. Pept. Sci. 15 (3): 175–83. doi:10.1002/psc.1091. PMID19035567.
