Fig. 5
From: Structural insights into SorCS2–Nerve Growth Factor complex formation
sSorCS2–NGF and unliganded sSorCS2 adopt different conformations. SorCS2 in complex with NGF has a different conformation and is more compact compared to the unliganded sSorCS2 structure. a, b domain rearrangement scheme of the conformational plasticity between unliganded (a) and liganded SorCS2 (b). Dimensions of the sSorCS2 dimers and angle between the PKD2 domains are indicated. NGF has been omitted for clarity. c cartoon representation of the unliganded SorCS2 homodimer in an orientation similar to (a) and in a 50° rotated view. The β-propellers are positioned at an angle with their ligand-binding top face close to the cell surface. d sSorCS2–NGF complex representation identical to (c). NGF is now shown (colored beige). In the NGF-bound structure, the β-propellers have moved up and away from the cell surface exposing the top face
