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Like most GPCRs, the AT1R signals through two transducers, G proteins and \u03b2-arrestins\n                  <jats:sup>2,3<\/jats:sup>\n                  . Previous reports have described \u03b2-arrestin-biased\n                  <jats:italic>peptide orthosteric<\/jats:italic>\n                  agonists for the AT1R with potential therapeutic advantages over currently available unbiased ARBs\n                  <jats:sup>4\u20136<\/jats:sup>\n                  . Here we report the DNA- encoded library screening-guided isolation and pharmacological characterization of the first\n                  <jats:italic>small molecule AT1R allosteric<\/jats:italic>\n                  ligands. We use cryo-electron microscopy, double electron- electron resonance spectroscopy, molecular dynamics simulations, and targeted mutagenesis to determine their binding sites, binding modes and conformational mechanisms driving their unique and divergent modulatory effects on G protein and \u03b2-arrestin pathways. Our findings uncover new mechanisms for precisely controlling the dynamic behavior of the AT1R with implications for drug development targeting this pathophysiologically important receptor family.\n                <\/jats:p>","DOI":"10.64898\/2026.07.15.736838","type":"posted-content","created":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T14:38:35Z","timestamp":1784212715000},"source":"Crossref","is-referenced-by-count":0,"title":["Conformational Basis of Functionally Selective Allosteric Modulation of the Angiotensin II type 1 Receptor by Small Molecules"],"prefix":"10.64898","author":[{"given":"Samuel","family":"Liu","sequence":"first","affiliation":[{"name":"Department of Medicine, Duke University School of Medicine, Durham, NC 27710, USA"},{"name":"University of Texas Medical Scientist Training Program at Houston, University of Texas Health Science Center at Houston, Houston, TX 77030, 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