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. 2019 Jun;19(16):1399–1417. doi: 10.2174/1568026619666190709092647

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© 2019 Bentham Science Publishers

This is an open access article licensed under the terms of the Creative Commons Attribution-Non-Commercial 4.0 International Public License (CC BY-NC 4.0) (https://creativecommons.org/licenses/by-nc/4.0/legalcode), which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

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Fig. (4) — (A) Overlapped ECD structures of five class B GPCRs in complex with their peptide ligands (PDBIDs: 2QKH (GIP receptor), 3IOL (GLP-1 receptor), 3C4M (PTHR), 2L27 (CRF receptor with α-helical CRF), 3N96 (CRF receptor with urocortin) [34-37]. A three-layered α1-(β1-β2)-(β3-β4)/α2 fold is presented. (B) The full-length crystal structure of GCGR in complex with a glucagon analogue [13], in comparison with the full-length cryo-EM structure of the CGRP receptor. The CGRP receptor is shown in association with its receptor associated modifying protein 1 (RAMP1). (C) The PACAP-bound PAC1R ECD model. (D) Hypothetical models of full-length PAC1R bound to PACAP in open- and closed-states.