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https://doi.org/10.1371/journal.pone.0019682
Title: | Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors | Authors: | Kumar, S. Pioszak, A. Zhang, C. Swaminathan, K. Xu, H.E. |
Issue Date: | 2011 | Citation: | Kumar, S., Pioszak, A., Zhang, C., Swaminathan, K., Xu, H.E. (2011). Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors. PLoS ONE 6 (5) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0019682 | Abstract: | Pituitary adenylate cyclase activating polypeptide (PACAP) is a member of the PACAP/glucagon family of peptide hormones, which controls many physiological functions in the immune, nervous, endocrine, and muscular systems. It activates adenylate cyclase by binding to its receptor, PAC1R, a member of class B G-protein coupled receptors (GPCR). Crystal structures of a number of Class B GPCR extracellular domains (ECD) bound to their respective peptide hormones have revealed a consensus mechanism of hormone binding. However, the mechanism of how PACAP binds to its receptor remains controversial as an NMR structure of the PAC1R ECD/PACAP complex reveals a different topology of the ECD and a distinct mode of ligand recognition. Here we report a 1.9 Å crystal structure of the PAC1R ECD, which adopts the same fold as commonly observed for other members of Class B GPCR. Binding studies and cell-based assays with alanine-scanned peptides and mutated receptor support a model that PAC1R uses the same conserved fold of Class B GPCR ECD for PACAP binding, thus unifying the consensus mechanism of hormone binding for this family of receptors. © 2011 Kumar et al. | Source Title: | PLoS ONE | URI: | http://scholarbank.nus.edu.sg/handle/10635/100368 | ISSN: | 19326203 | DOI: | 10.1371/journal.pone.0019682 |
Appears in Collections: | Staff Publications Elements |
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