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. 2004 Aug;15(8):3520–3529. doi: 10.1091/mbc.E04-02-0093

Figure 6.

Figure 6.

PD blocks activity of Abl-WT but not Abl-T315I. (A and B) Crystal structure of PD-166326 in the ATP-binding pocket of Abl-WT (A) and Abl-T315I (B). Structure shows van der Waals interactions between T315 (blue in A) and PD. Ile substitution for Thr at position 315 (red in B) results in disruption of van der Waals interactions, steric hindrance, and loss of binding. (C) PD-166326 blocks kinase activity of Abl-WT but not Abl-T315I. Analysis of kinase activity in untransfected 293 cells (lanes 1 and 2) or in 293 cells transiently transfected with Abl-WT (lanes 3 and 4) or Abl-T315I (lanes 5 and 6). Transfected Abl was immunoprecipitated with α-Abl mAb AB3 and incubated with GST-Crk and ATP, together with DMSO (lanes 1, 3, and 5) or 10 nM PD-166326 (lanes 2, 4, and 6). No kinase activity from endogenous Abl was detectable in these cells. An equivalent amount of Abl immunoprecipitated from cells transfected with Abl-WT or Abl-T315I (see below). PD blocked kinase activity of precipitates from Abl-WT cells (lane 4), but not Abl-T315I cells.