Crystal Structure of the PAC1R Extracellular Domain Unifies a Consensus Fold for Hormone Recognition by Class B G-Protein Coupled Receptors
Figure 2
(a)(i) The ribbon diagram of the PAC1R ECD. Strands β1 and β2 make an anti-parallel β-sheet and strands β3, β4 and β5 make another anti-parallel β-sheet. (b) The stereo view of the electron density around the conserved residues that form the core of the PAC1R structure. The density is contoured at the 2σ level. (c) Stereo view of the electron density for the C77–C113 disulphide bond and the residues around it contoured at 1 σ. The residues are as labelled. The electron density obtained for the β3–β4 loop is clean allowing even the side chains to be discerned clearly.