NDLI: Activation induces structural changes in the liganded angiotensin II type 1 receptor.

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Activation induces structural changes in the liganded angiotensin II type 1 receptor.

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Activation induces structural changes in the liganded angiotensin II type 1 receptor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lavigne, Pierre Clément, Martin Leduc, Richard Guillemette, Gaétan Holleran, Brian J. Cabana, Jérôme Escher, Emanuel
Description	Author Affiliation: Clément M ( Department of Pharmacology, Faculty of Medicine, Université de Sherbrooke, Sherbrooke, Quebec J1H 5N4, Canada.)
Abstract	The octapeptide hormone angiotensin II (AngII) binds to and activates the human angiotensin II type 1 receptor (hAT(1)) of the G protein-coupled receptor class A family. Several activation mechanisms have been proposed for this family, but they have not yet been experimentally validated. We previously used the methionine proximity assay to show that 11 residues in transmembrane domain (TMD) III, VI, and VII of the hAT(1) receptor reside in close proximity to the C-terminal residue of AngII. With the exception of a single change in TMD VI, the same contacts are present on N111G-hAT(1), a constitutively active mutant; this N111G-hAT(1) is a model for the active form of the receptor. In this study, two series of 53 individual methionine mutations were constructed in TMD I, II, IV, and V on both receptor forms. The mutants were photolabeled with a neutral antagonist, (125)I-[Sar(1),p-benzoyl-L-Phe(8)]AngII, and the resulting complexes were digested with cyanogen bromide. Although no new contacts were found for the hAT(1) mutants, two were found in the constitutively active mutants, Phe-77 in TMD II and Asn-200 in TMD V. To our knowledge, this is the first time that a direct ligand contact with TMD II and TMD V has been reported. These contact point differences were used to identify the structural changes between the WT-hAT(1) and N111G-hAT(1) complexes through homology-based modeling and restrained molecular dynamics. The model generated revealed an important structural rearrangement of several TMDs from the basal to the activated form in the WT-hAT(1) receptor.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	39
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-09-25
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Angiotensin II Metabolism Mutation Receptor, Angiotensin, Type 1 Amino Acid Sequence Animals Binding Sites Genetics COS Cells Cercopithecus Aethiops Cyanogen Bromide Chemistry Electrophoresis, Polyacrylamide Gel Inositol Phosphates Ligands Methionine Models, Biological Molecular Sequence Data Mutagenesis, Site-Directed Photoaffinity Labels Protein Binding Transfection Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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