Fig. 2: Conformational changes in TrkA monomer and tetramer. | Nature Communications

Fig. 2: Conformational changes in TrkA monomer and tetramer.

From: TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential

Fig. 2

a–c TrkA gating ring from TrkHA-ADP (a), TrkHA-ATPγS (b), and TrkHA-ATP (c), viewed from the periplasmic (top), N2-N2 interface (middle), and N1-N1 interface (bottom) sides. The 2Fo-Fc electron density maps of N2-N2 and N1-N1 interfaces are shown as blue mesh contoured at 1.0σ on the right. d Conformational changes within a TrkA protomer. N1 and N2 domains of a TrkA protomer from TrkHA-ADP (blue), TrkHA-ATPγS (orange), TrkHA-ATP (red), or TrkHA-NADH (green) are render in ribbons. The N1 domains were superimposed to show the relative rotations of the N2 domain.

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