Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/25819
Title: Crystal structure of PacIR Extracelluar Domain: Insights of Hormone Recognition
Authors: SHIVA KUMAR
Keywords: Crystal structure, GPCR, PAC1R, PACAP, Membrane protein, peptide hormone
Issue Date: 21-Dec-2010
Source: SHIVA KUMAR (2010-12-21). Crystal structure of PacIR Extracelluar Domain: Insights of Hormone Recognition. ScholarBank@NUS Repository.
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 a 1.9 ? crystal structure of the PAC1R ECD is reported, which adopts the same fold as commonly observed for other members of Class B GPCR. Binding studies with alanine-scanned peptides and mutated receptor ECD 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.
URI: http://scholarbank.nus.edu.sg/handle/10635/25819
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