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. Author manuscript; available in PMC: 2009 Aug 3.
Published in final edited form as: Cancer Cell. 2008 Aug 12;14(2):180–192. doi: 10.1016/j.ccr.2008.06.014

Figure 2. p110α gatekeeper mutants have reduced catalytic activity.

Figure 2

A: Sequence alignment of p110α with protein kinases that display clinical resistance mutations at the gatekeeper position

B: ATP binding sites of Abl (PDB code 2G1T) and p110α (PDB code 2RD0). ATP from p110γ co-crystal (PDB code 1E8X) was overlaid onto the apo p110α structure by structural alignment. The gatekeeper residue is colored red and labeled in both structures.

C: Six-fold serial dilutions of YRP1-pURA3-2μ-GAL1-p110αH1047R-CAAX strains with the indicated p110α mutations were spotted onto agar plates of SD −URA media containing either glucose or galactose. The plates were incubated at 30°C for 2 days (glucose) and 6 days (galactose).

D: Distribution of residues at the gatekeeper position in the human PI3K and protein kinase families.