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. Author manuscript; available in PMC: 2015 Dec 12.
Published in final edited form as: J Mol Biol. 2014 Aug 29;426(24):3985–4001. doi: 10.1016/j.jmb.2014.08.014

Figure 6. Proposed models of paxillin133–290 binding to the FAT domain of FAK and the FAT domain of Pyk2.

Figure 6

(A) In Pyk2-FAT, the LD2 and LD4 motifs of paxillin133–290 undergo a conformational switching mechanism in which two discrete conformations of paxillin compete for binding; one with LD2 occupying H1/H4 and LD4 occupying H2/H3, and the other conformation with LD4 at H1/H4 and LD2 at H2/H3. (B) In FAT, the LD2 and LD4 motifs of paxillin133–290 binds to opposite faces of the four-helix bundle (H2/H3 and H1/H4) and are oriented in the same direction.