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Photoprobe Peptides to Map the Interactions of Angiotensin II with its Receptor AT1

  • D. Fillion
  • G. Guillemette
  • R. Leduc
  • E. Escher
Part of the Advances in Experimental Medicine and Biology book series (volume 611)

Introduction

Seven transmembrane domains (TMDs) G protein-coupled receptors (GPCRs) are the largest family of cell surface receptors and are implicated in various pathologies. In fact, those proteins are privileged targets in pharmacotherapy since approximatively 50% of all current market drugs act via these receptors. The rational design of drugs targeting GPCRs requires a 3D molecular-based knowledge of those proteins that may be acquired by identification of ligand-receptor interactions through photoaffinity labeling [1]. This approach allows to directly map the ligand-receptor interface by covalent bonding of the radio-labeled photoprobe ligand within the immediate molecular surroundings of its cognate receptor. This information may then be used in conjunction with computational molecular modeling procedures, based on the X-ray crystallography of bovine rhodopsin, to build and validate homology molecular models of receptors with ligand [2]. In the present contribution, we have...

Keywords

Proteinaceous Material Bovine Rhodopsin Photoaffinity Label Helical Bundle Neutral Antagonist 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

This ongoing study is funded by the Canadian Institutes of Health Research (CIHR) and the Quebec chapter of the Heart and Stroke Foundation of Canada (HSFC) to G.G., R.L. and E.E.

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Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • D. Fillion
    • 1
  • G. Guillemette
    • 1
  • R. Leduc
    • 1
  • E. Escher
    • 1
  1. 1.Faculty of Medecine & Health Sciences, Department of PharmacologyUniversité de SherbrookeSherbrooke, QuébecCanada

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