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Intra- and inter-domain rearrangements underly the function of VPS10 family members. (A) Substantial conformational changes are apparent within the Sortilin β-propeller in changing from the monomer form (blue, pdb 3f6k) to the dimer form (red, pdb 5nmt). The 10 Sortilin β-propeller blades are numbered. (B) The SorCS2 dimer changes its conformation, predominantly by domain rearrangements, upon ligand binding (unbound, pdb 6ffy and bound, pdb 6fg9).
