Skip to main content
. Author manuscript; available in PMC: 2018 Mar 1.
Published in final edited form as: Nature. 2017 Apr 24;546(7656):118–123. doi: 10.1038/nature22327

Figure 3. Comparisons of inactive class B and the activated CTR structures.

Figure 3

a, Side (left), extracellular (middle) and cytoplasmic (right) views of the sCT/CTR/Gs (blue) relative to inactive CRF-1R (PDB: 4Z9G, yellow) and GCGR (PDB: 5EE7, purple) structures. Differences in TMs at the extracellular and cytoplasmic faces are highlighted. b, The positions of class B conserved polar residues located within the activated CTR bundle (left), the inactive GCGR (middle) and the CP-376395 bound CRF-1R (right). The central polar network likely forms interactions in all structures, while the TM2-3-6-7 and TM2-6-7-H8 networks that stabilise class B inactive structures (as in the GCGR) are disrupted in the activated CTR. In the CRF-1R, CP-376395 binding also disrupts these interactions.