Engineering and biophysical analysis of alpha adrenergic receptor crystallography constructs

Public Deposited
Analytics

Downloadable Content

Download PDF
Request Version for Screen Reader
Last Modified
  • March 19, 2019
Creator
  • Schools, Zachary
    • Affiliation: School of Medicine, Department of Pharmacology
Abstract
  • G protein-coupled receptors (GPCRs) are ubiquitously expressed membrane-spanning proteins that control all of human physiology. GPCRs are structurally complex and their mechanism of activation and signaling is not fully understood. Furthermore, there is a need for more subtype-selective and functionally selective drugs. Development of these drugs could be accelerated by obtaining crystal structures of GPCRs. One such family that could benefit from the structural information in a crystal structure is the Alpha Adrenergic receptors (ADRA). ADRA receptors control cardiovascular as well as peripheral and central nervous system functions, but lack subtype selective drugs. Thus, the ADRA receptor family was screened in parallel for thermostability and likelihood of crystal formation. ADRA1A-nBRIL bound to prazosin was found to be the best target for further crystallization efforts.
Date of publication
Keyword
DOI
Resource type
Rights statement
  • In Copyright
Advisor
  • Roth, Bryan
  • Nicholas, Robert
  • Graves, Lee
Degree
  • Master of Science
Degree granting institution
  • University of North Carolina at Chapel Hill Graduate School
Graduation year
  • 2016
Language

Relations

Parents:

This work has no parents.

Items

Thumbnail Title Date Uploaded Visibility Actions
file details Schools_unc_0153M_16485.pdf 2019-04-10 Public Download