Structure of Tel, Abl, and chimeric Tel-Abl and Bcr-Abl proteins.

(A) Full-length Tel (ETV6) protein of 452 amino acids, with positions of the PNT homology oligomerization domain and ETS DNA-binding domain indicated by dark shaded boxes. (B) Full-length type Ib c-Abl protein of 1142 amino acids, with NH₂-terminal myristoylation site, SH3 and SH2 domains, tyrosine kinase catalytic domain, and COOH-terminal DNA- and actin-binding domains indicated by lightly shaded boxes. (C) Tel-Abl fusion protein, consisting of sequences fromTEL exons 1 to 5 (amino acids 1-336) fused to the COOH-terminal 1104 amino acids of Abl. (D) Tel-Abl K581R mutant, containing an inactivating point mutation in the Abl catalytic domain of lysine 581 to arginine. (E) Tel-Abl ΔPNT, with an inframe deletion of 76 amino acids between Eco47III and XmnI sites11 resulting in loss of most of the PNT domain. (F) The p210 Bcr-Abl fusion protein, consisting of Bcr amino acids 1 to 927 fused to the COOH-terminal 1104 amino acids of Abl, with the NH₂-terminal coiled-coil (CC) domain and region of homology to Dbl-Cdc42 designated by black boxes and the location of the tyrosine 177 Grb2 binding site indicated.