| 词条 | CFC domain |
| 释义 |
| Symbol = CFC | Name = CFC | image = PDB 2j5h EBI.jpg | width = | caption = nmr analysis of mouse cripto cfc domain | Pfam = PF09443 | Pfam_clan = | InterPro = IPR019011 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} 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 binds Alk4 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] References1. ^1 2 {{cite journal |vauthors=Foley SF, van Vlijmen HW, Boynton RE, Adkins HB, Cheung AE, Singh J, Sanicola M, Young CN, Wen D | title = The CRIPTO/FRL-1/CRYPTIC (CFC) domain of human Cripto. Functional and structural insights through disulfide structure analysis | journal = Eur. J. Biochem. | volume = 270 | issue = 17 | pages = 3610–8 |date=September 2003 | pmid = 12919325 | doi = 10.1046/j.1432-1033.2003.03749.x| url = }} {{InterPro content|IPR019011}}2. ^{{cite journal |vauthors=Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M | title = Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala | journal = J. Med. Chem. | volume = 49 | issue = 24 | pages = 7054–62 |date=November 2006 | pmid = 17125258 | doi = 10.1021/jm060772r | url = }} 3. ^{{cite journal |vauthors=Calvanese L, Saporito A, Oliva R, D' Auria G, Pedone C, Paolillo L, Ruvo M, Marasco D, Falcigno L | title = Structural insights into the interaction between the Cripto CFC domain and the ALK4 receptor | journal = J. Pept. Sci. | volume = 15 | issue = 3 | pages = 175–83 |date=March 2009 | pmid = 19035567 | doi = 10.1002/psc.1091 | url = }} 1 : Protein domains |
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