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000275871 0247_ $$2doi$$a10.1016/j.cell.2015.04.011
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000275871 1001_ $$0P:(DE-HGF)0$$aZhang, Haitao$$b0
000275871 245__ $$aStructure of the Angiotensin Receptor Revealed by Serial Femtosecond Crystallography
000275871 260__ $$a[Cambridge, Mass.]$$bCell Press$$c2015
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000275871 500__ $$a(c) Elsevier Inc. 
000275871 520__ $$aAngiotensin II type 1 receptor (AT1R) is a G protein-coupled receptor that serves as a primary regulator for blood pressure maintenance. Although several anti-hypertensive drugs have been developed as AT1R blockers (ARBs), the structural basis for AT1R ligand-binding and regulation has remained elusive, mostly due to the difficulties of growing high-quality crystals for structure determination using synchrotron radiation. By applying the recently developed method of serial femtosecond crystallography at an X-ray free-electron laser, we successfully determined the room-temperature crystal structure of the human AT1R in complex with its selective antagonist ZD7155 at 2.9-Å resolution. The AT1R-ZD7155 complex structure revealed key structural features of AT1R and critical interactions for ZD7155 binding. Docking simulations of the clinically used ARBs into the AT1R structure further elucidated both the common and distinct binding modes for these anti-hypertensive drugs. Our results thereby provide fundamental insights into AT1R structure-function relationship and structure-based drug design.
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000275871 7001_ $$0P:(DE-HGF)0$$aUnal, Hamiyet$$b1
000275871 7001_ $$0P:(DE-H253)PIP1017962$$aGati, Cornelius$$b2
000275871 7001_ $$0P:(DE-HGF)0$$aHan, Gye Won$$b3
000275871 7001_ $$0P:(DE-H253)PIP1021486$$aLiu, Wei$$b4
000275871 7001_ $$0P:(DE-HGF)0$$aZatsepin, Nadia A.$$b5
000275871 7001_ $$0P:(DE-HGF)0$$aJames, Daniel$$b6
000275871 7001_ $$0P:(DE-HGF)0$$aWang, Dingjie$$b7
000275871 7001_ $$0P:(DE-HGF)0$$aNelson, Garrett$$b8
000275871 7001_ $$0P:(DE-H253)PIP1008265$$aWeierstall, Uwe$$b9
000275871 7001_ $$0P:(DE-HGF)0$$aSawaya, Michael R.$$b10
000275871 7001_ $$0P:(DE-HGF)0$$aXu, Qingping$$b11
000275871 7001_ $$0P:(DE-H253)PIP1005807$$aMesserschmidt, Marc$$b12
000275871 7001_ $$0P:(DE-HGF)0$$aWilliams, Garth J.$$b13
000275871 7001_ $$0P:(DE-H253)PIP1009086$$aBoutet, Sébastien$$b14
000275871 7001_ $$0P:(DE-HGF)0$$aWang, Chong$$b15
000275871 7001_ $$0P:(DE-HGF)0$$aIshchenko, Andrii$$b16
000275871 7001_ $$0P:(DE-HGF)0$$aTirupula, Kalyan C.$$b17
000275871 7001_ $$0P:(DE-HGF)0$$aDesnoyer, Russell$$b18
000275871 7001_ $$0P:(DE-H253)PIP1027479$$aCoe, Jesse$$b19
000275871 7001_ $$0P:(DE-HGF)0$$aConrad, Chelsie E.$$b20
000275871 7001_ $$0P:(DE-H253)PIP1023170$$aFromme, Petra$$b21
000275871 7001_ $$0P:(DE-HGF)0$$aStevens, Raymond C.$$b22
000275871 7001_ $$0P:(DE-HGF)0$$aKatritch, Vsevolod$$b23
000275871 7001_ $$0P:(DE-HGF)0$$aKarnik, Sadashiva S.$$b24
000275871 7001_ $$0P:(DE-HGF)0$$aCherezov, Vadim$$b25$$eCorresponding author
000275871 7001_ $$0P:(DE-H253)PIP1006155$$aYefanov, Oleksandr$$b26$$udesy
000275871 7001_ $$0P:(DE-H253)PIP1010779$$aWhite, Thomas$$b27$$udesy
000275871 773__ $$0PERI:(DE-600)2001951-8$$a10.1016/j.cell.2015.04.011$$gVol. 161, no. 4, p. 833 - 844$$n4$$p833 - 844$$tCell$$v161$$x0092-8674$$y2015
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