Figure 3.

(a) Structural features of the FGF polypeptide. The amino terminus of some FGFs contains a signal sequence (shaded). All FGFs contain a core region that contains conserved amino-acid residues and conserved structural motifs. The locations of β strands within the core region are numbered and shown as black boxes. The heparin-binding region (pink) includes residues in the loop between β strands 1 and 2 and in β strands 10 and 11. Residues that contact the FGFR are shown in green (the region contacting Ig-domain 2 of the receptor), blue (contacting Ig-domain 3) and red (contacting the alternatively spliced region of Ig-domain 3). Amino-acid residues that contact the linker region are shown in gray [20]. (b) Three-dimensional structure of FGF2, a prototypical member of the FGF family. A ribbon diagram of FGF2 is shown; β strands are labeled 1-12 and regions of contact with the FGFR and heparin are color-coded as in (a) [22,24]. Image provided by M. Mohammadi.

Ornitz and Itoh Genome Biology 2001 2:reviews3005.1-reviews3005.12   doi:10.1186/gb-2001-2-3-reviews3005