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Fig. 4. (A) View of Cripto model superimposed onto the basic FGF structure (2bfh). The C{alpha} traces are shown. The Cripto and 2bfh traces are rendered in magenta and cyan, respectively. The r.m.s.d. of the backbone atoms (C, C-alfa and N atoms) for the two superimposed structures was 0.91Å on a total of 468 corresponding atoms. (B) Cripto model (C{alpha} trace) with highlighted EGF (red) and CFC (blue) regions. The disulphide bonds (in yellow) are also shown. (C) Ribbon rendering of the Cripto model with all mutated residues drawn with a CPK representation. Mutations with a strong and less severe effect are indicated in blue and cyan, respectively while ineffective mutations are indicated in red. ß-strands are shown as green arrows and loops as yellow ropes. Orientation is different from A and B.





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