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. 2005 Mar 21;102(13):4747–4752. doi: 10.1073/pnas.0406039102

Fig. 6.

Fig. 6.

Allosteric model of PLN interaction with SERCA. PLN monomer interconverts between the bent form (T state) and the less stable (more dynamically disordered) extended form (R state). The T state inhibits SERCA because of its interaction in the transmembrane domain. Only in the R state, in which the cytoplasmic domains interact, is SERCA-bound PLN capable of reversing SERCA inhibition, because of PLN phosphorylation or mutation. SERCA has a greater affinity for the R form and thus shifts the equilibrium toward this regulatory intermediate.