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. 2014 Jan 16;10(1):e1003435. doi: 10.1371/journal.pcbi.1003435

Figure 6. Number of P-sites in proximity of the catalytic site in randomized EGFR structural models.

Figure 6

The set of five hundred dimeric EGFR structures with randomized CT domain conformations was analyzed to determine the number of structures that had a given P-site tyrosine residue within 40 Å of the γ-phosphate of the AMPPMP substrate bound in the catalytic site. The kinase-proximal site P-site-992 of the receiver molecule was most often and that of the activator molecule least often near the catalytic site, consistent with the bias for cis versus trans P-site-992 binding events in simulations (cf. Fig. 4). This cis-trans bias, as well as the number in proximity of the catalytic site, was markedly reduced for P-sites more distal to the kinase core.