Control of Genetically Prescribed Protein Tyrosine Kinase Activities by Environment-Linked Redox Reactions
Figure 1
Shematic illustration of structures of human c-SRC and human c-RET kinase proteins. Primary and tertiary structures of c-SRC (PDB 2SRC) and c-RET (PDB 2IVS) are deduced from the data in Protein Data Bank (PDB). (a) Primary structures of c-SRC (top) and c-RET (bottom) kinase domains. α: α-helix; β: β-sheet. (b) Tertiary structures of SH3, SH2, and kinase (N-lobe and C-lobe) domains of c-SRC (left) and kinase domain of c-RET (right). Positions of Tyr416 of c-SRC and Tyr905 of c-RET as major autophosphorylation sites and those of Cys277/Cys498 of c-SRC and Cys987 of c-RET (equivalent to Cys376 of RET-PTC-1) as well as positions of N-terminal (N) and C-terminal (C) amino acids are shown.
