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| 024 | 7 | _ | |a 10.1016/j.cell.2015.04.011 |2 doi |
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| 100 | 1 | _ | |a Zhang, Haitao |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Structure of the Angiotensin Receptor Revealed by Serial Femtosecond Crystallography |
| 260 | _ | _ | |a [Cambridge, Mass.] |c 2015 |b Cell Press |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
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| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1461937913_19568 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 500 | _ | _ | |a (c) Elsevier Inc. |
| 520 | _ | _ | |a Angiotensin II type 1 receptor (AT1R) is a G protein-coupled receptor that serves as a primary regulator for blood pressure maintenance. Although several anti-hypertensive drugs have been developed as AT1R blockers (ARBs), the structural basis for AT1R ligand-binding and regulation has remained elusive, mostly due to the difficulties of growing high-quality crystals for structure determination using synchrotron radiation. By applying the recently developed method of serial femtosecond crystallography at an X-ray free-electron laser, we successfully determined the room-temperature crystal structure of the human AT1R in complex with its selective antagonist ZD7155 at 2.9-Å resolution. The AT1R-ZD7155 complex structure revealed key structural features of AT1R and critical interactions for ZD7155 binding. Docking simulations of the clinically used ARBs into the AT1R structure further elucidated both the common and distinct binding modes for these anti-hypertensive drugs. Our results thereby provide fundamental insights into AT1R structure-function relationship and structure-based drug design. |
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