ArticleThe Journal of biological chemistry2013
Structure of the human angiotensin II type 1 (AT1) receptor bound to angiotensin II from multiple chemoselective photoprobe contacts reveals a unique peptide binding mode.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 46 citations in OpenAlex.
- The chemokine receptor-like fourth extracellular loop of the apelin receptor differentially regulates apelin and elabela binding and signalling.British journal of pharmacology · 2026Article
- Advances in the allostery of angiotensin II type 1 receptor.Cell & bioscience · 2023Review
- The Angiotensin ATPharmacological reviews · 2022Review
- Structural perspectives on the mechanism of signal activation, ligand selectivity and allosteric modulation in angiotensin receptors: IUPHAR Review 34.British journal of pharmacology · 2022Review
- Molecular Effects of Auto-Antibodies on Angiotensin II Type 1 Receptor Signaling and Cell Proliferation.International journal of molecular sciences · 2022Article
- Angiotensin and Endothelin Receptor Structures With Implications for Signaling Regulation and Pharmacological Targeting.Frontiers in endocrinology · 2022Review
- Signal Transduction of Mineralocorticoid and Angiotensin II Receptors in the Central Control of Sodium Appetite: A Narrative Review.International journal of molecular sciences · 2021Review
- Structural insights into ligand recognition and activation of angiotensin receptors.Trends in pharmacological sciences · 2021Review
- Insights into the Interaction of LVV-Hemorphin-7 with Angiotensin II Type 1 Receptor.International journal of molecular sciences · 2020Article
- Genetic code expansion and photocross-linking identify different β-arrestin binding modes to the angiotensin II type 1 receptor.The Journal of biological chemistry · 2019Article
- Mechanism of Hormone Peptide Activation of a GPCR: Angiotensin II Activated State of ATJournal of chemical information and modeling · 2019Article
- Distinctive Activation Mechanism for Angiotensin Receptor Revealed by a Synthetic Nanobody.Cell · 2019Article
- Divergent Spatiotemporal Interaction of Angiotensin Receptor Blocking Drugs with Angiotensin Type 1 Receptor.Journal of chemical information and modeling · 2018Article
- Current topics in angiotensin II type 1 receptor research: Focus on inverse agonism, receptor dimerization and biased agonism.Pharmacological research · 2017Review
- The importance of non-HLA antibodies in transplantation.Nature reviews. Nephrology · 2016Review
- International Union of Basic and Clinical Pharmacology. XCIX. Angiotensin Receptors: Interpreters of Pathophysiological Angiotensinergic Stimuli [corrected].Pharmacological reviews · 2015Review
- Identification of Distinct Conformations of the Angiotensin-II Type 1 Receptor Associated with the Gq/11 Protein Pathway and the β-Arrestin Pathway Using Molecular Dynamics Simulations.The Journal of biological chemistry · 2015Article
- Rational drug design and synthesis of molecules targeting the angiotensin II type 1 and type 2 receptors.Molecules (Basel, Switzerland) · 2015Review
- Electronic sculpting of ligand-GPCR subtype selectivity: the case of angiotensin II.ACS chemical biology · 2014Article
- Novel molecular angiotensin converting enzyme and angiotensin receptor imaging techniques.Current cardiology reports · 2014Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Breakthroughs in G protein-coupled receptor structure determination based on crystallography have been mainly obtained from receptors occupied in their transmembrane domain core by low molecular weight ligands, and we have only recently begun to elucidate how the extracellular surface of G protein-coupled receptors (GPCRs) allows for the binding of larger peptide molecules. In the present study, we used a unique chemoselective photoaffinity labeling strategy, the methionine proximity assay, to directly identify at physiological conditions a total of 38 discrete ligand/receptor contact residues that form the extracellular peptide-binding site of an activated GPCR, the angiotensin II type 1 receptor. This experimental data set was used in homology modeling to guide the positioning of the angiotensin II (AngII) peptide within several GPCR crystal structure templates. We found that the CXC chemokine receptor type 4 accommodated the results better than the other templates evaluated; ligand/receptor contact residues were spatially grouped into defined interaction clusters with AngII. In the resulting receptor structure, a β-hairpin fold in extracellular loop 2 in conjunction with two extracellular disulfide bridges appeared to open and shape the entrance of the ligand-binding site. The bound AngII adopted a somewhat vertical binding mode, allowing concomitant contacts across the extracellular surface and deep within the transmembrane domain core of the receptor. We propose that such a dualistic nature of GPCR interaction could be well suited for diffusible linear peptide ligands and a common feature of other peptidergic class A GPCRs.
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