Presentation Title

Molecular Dynamics Study of the Pituitary Adenylate Cyclase-Activating Polypeptide Binding to the Pituitary Adenylate Cyclase Type I Receptor

Start Date

November 2016

End Date

November 2016

Location

HUB 302-6

Type of Presentation

Poster

Abstract

The pituitary adenylate cyclase-activating polypeptide (PACAP) is a peptide hormone, which binds to the pituitary adenylate cyclase type I (PAC1) receptor, and is recognized as a factor with pleiotropic physiological functions in many different organ systems. The PAC1R receptor is a G-protein coupled receptor and is part of the glucagon superfamily. The structure for the ectodomains of PAC1 receptor has been determined by nuclear magnetic resonance (NMR) and x-ray crystallography. However, the binding pose of PACAP remains debatable as the structure from NMR shows different topology from the structure derived from x-ray crystallography. In this study, we used molecular dynamic simulations to effectively understand the most stable and reliable interaction between this neuropeptide and its receptor. The binding pocket of PAC1 and interaction between PACAP and PAC1 receptor will be used to design PAC1 receptor peptidomimetics and small molecular antagonists.

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Molecular Dynamics Study of the Pituitary Adenylate Cyclase-Activating Polypeptide Binding to the Pituitary Adenylate Cyclase Type I Receptor

HUB 302-6

The pituitary adenylate cyclase-activating polypeptide (PACAP) is a peptide hormone, which binds to the pituitary adenylate cyclase type I (PAC1) receptor, and is recognized as a factor with pleiotropic physiological functions in many different organ systems. The PAC1R receptor is a G-protein coupled receptor and is part of the glucagon superfamily. The structure for the ectodomains of PAC1 receptor has been determined by nuclear magnetic resonance (NMR) and x-ray crystallography. However, the binding pose of PACAP remains debatable as the structure from NMR shows different topology from the structure derived from x-ray crystallography. In this study, we used molecular dynamic simulations to effectively understand the most stable and reliable interaction between this neuropeptide and its receptor. The binding pocket of PAC1 and interaction between PACAP and PAC1 receptor will be used to design PAC1 receptor peptidomimetics and small molecular antagonists.