Protein Structure from Scientific Research

Extracellular (b) and intracellular (c) views of the superimposed TMDs of PCO371-bound active PTH1R, PTH-bound active PTH1R and ePTH-bound inactive PTH1R. b , Two-way arrows indicate distances of C atoms of Thr192 1.44 (TM1), Ile422 6.54 (TM6) and Met445 7.43 (TM7) residues between the structures of PCO371-bound PTH1R and PTH-bound active PTH1R, or between the structures of PCO371-bound and ePTH-bound inactive-like PTH1R.

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