Cbp

The binding of ATP to its site at the TK domain of EGFR was initially studied by molecular modelling techniques, based on the X-ray crystal structure of the complex between the related cAMP-dependent PTK, an inhibitor, Mg, and ATP. This binding involves two hydrogen bonds at the Gln-767 and Met-769, among other interactions. The ribose unit binds to its own pocket, and the triphosphate chain is placed in a cleft that leads to the surface of the enzyme (Fig. 9.8A). This active site also contains unoccupied spaces, especially a hydrophobic pocket opposite to the place where the ribose binds. This pocket shows slight differences

Gln-767

H2NOC

Hydrophobic pocket

Leu-768

H3C H3C

Met-769

Gln-767

H2NOC

Hydrophobic pocket

Leu-768

H3C H3C

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