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Figure 2.
FIGURE 2. RET kinase structures. A, RET-KD-P (green) and
RET-KD-0P (cyan for molecule A and red for molecule B)
structures superimposed using the C-lobe C-  atoms. The bound
nucleotides are shown as sticks. B, RET-KD-P (green), activated
IRK (Protein Data Bank code 1IR3; orange), and Kit (Protein Data
Bank code 1PKG; blue) structures superimposed using equivalent
C-lobe C- atoms. C and D,
orthogonal views of the trans-inhibited RET-KD dimer with
molecule A in green and molecule B in light green. Their
N-terminal helices are red and cyan, respectively. Side chain
sticks are shown for Tyr^900 and Tyr^905 (orange), Met^918
(magenta), and Pro^766 (orange). E, main chain hydrogen bond
contacts in the complex structure (Protein Data Bank code 1IR3)
between IRK (orange) and substrate peptide (cyan). F, main chain
hydrogen bond contacts in RET-KD between the Met^918 pocket of
molecule A (green) and Pro^766 of molecule B (light green).
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