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. Author manuscript; available in PMC: 2009 May 27.
Published in final edited form as: Biochemistry. 2008 Apr 30;47(21):5681–5688. doi: 10.1021/bi8003044

FIGURE 3. Trans-phosphorylation of dimeric receptors.

FIGURE 3

(a) Reactions and equations describing the interactions of open-conformation E with dimeric receptor RR. The phosphorylation/dephosphorylation and association constants are as in Fig. 2, except k4 represents receptor trans-phosphorylation within a RR*-E complex. These reactions are solved in Appendix 2.

(b) Fractional receptor phosphorylation (fR) as a function of the control parameter for receptor phosphorylation (θR), for particular values of Q, Et/Rt and K3Rt. The control (red) is for monomeric receptors. Black lines show results for dimeric receptors with various values of the receptor trans-phosphorylation parameter (σ). Dimerization does not change any parameter except σ, which increases fR (red arrow).

(c) Relative increase in receptor phosphorylation due to dimerization.