Please use this identifier to cite or link to this item: 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
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