Evidence map›Paper›PMID 25913193›Full record

ArticleCell2015

Structure of the Angiotensin receptor revealed by serial femtosecond crystallography.

Haitao Zhang, Hamiyet Unal, Cornelius Gati, Gye Won Han, Wei Liu, Nadia A Zatsepin, Daniel James, Dingjie Wang, Garrett Nelson, Uwe Weierstall and 18 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 200 papers.

0numbers the graph read from it
0cells of the map it votes in
200citing papers in PubMed
24.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

200 citing papers in PubMed, 378 citations in OpenAlex.

  1. Article
  2. Article
  3. Activation of the angiotensin II type I receptor by a nonpeptide agonist.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  19. Epitope-directed selection of GPCR nanobody ligands with evolvable function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

140 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

28 authors at 11 institutions in 3 countries.

Haitao ZhangDepartment of Biological Sciences, Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.
Hamiyet UnalDepartment of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Cornelius GatiCenter for Free Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, 22607 Hamburg, Germany.
Gye Won HanDepartment of Chemistry, Bridge Institute, University of Southern California, Los Angeles, CA 90089 USA.
Wei LiuDepartment of Chemistry and Biochemistry, Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA.
Nadia A ZatsepinDepartment of Physics, Arizona State University, Tempe, AZ 85287, USA.
Daniel JamesDepartment of Physics, Arizona State University, Tempe, AZ 85287, USA.
Dingjie WangDepartment of Physics, Arizona State University, Tempe, AZ 85287, USA.
Garrett NelsonDepartment of Physics, Arizona State University, Tempe, AZ 85287, USA.
Uwe WeierstallDepartment of Physics, Arizona State University, Tempe, AZ 85287, USA.
Michael R SawayaDepartment of Chemistry and Biochemistry, the UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, CA 90095, USA.
Qingping XuJoint Center for Structural Genomics, Stanford Synchrotron Radiation Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Marc MesserschmidtBioXFEL Science and Technology Center, Buffalo, NY 14203, USA.
Garth J WilliamsLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Sébastien BoutetLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Oleksandr M YefanovCenter for Free Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, 22607 Hamburg, Germany.
Thomas A WhiteCenter for Free Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, 22607 Hamburg, Germany.
Chong WangDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Andrii IshchenkoDepartment of Chemistry, Bridge Institute, University of Southern California, Los Angeles, CA 90089 USA.
Kalyan C TirupulaDepartment of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Russell DesnoyerDepartment of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Jesse CoeDepartment of Chemistry and Biochemistry, Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA.
Chelsie E ConradDepartment of Chemistry and Biochemistry, Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA.
Petra FrommeDepartment of Chemistry and Biochemistry, Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA.
Raymond C StevensDepartment of Biological Sciences, Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA; Department of Chemistry, Bridge Institute, University of Southern California, Los Angeles, CA 90089 USA; iHuman Institute, ShanghaiTech University, Shanghai, 201210 China.
Vsevolod KatritchDepartment of Biological Sciences, Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.
Sadashiva S KarnikDepartment of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Vadim CherezovDepartment of Chemistry, Bridge Institute, University of Southern California, Los Angeles, CA 90089 USA. Electronic address: cherezov@usc.edu.
Arizona State University · USUniversity of Southern California · USCleveland Clinic Lerner College of Medicine · USCenter for Free-Electron Laser Science · DEBioXFEL Science and Technology Center · USHarvard University · USJoint Center for Structural Genomics · USLinac Coherent Light Source · USSLAC National Accelerator Laboratory · USUniversität Hamburg · DEUniversity of California, Los Angeles · US

Funding

Structure Determination Core at SSRLU54GM094586 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GODZIK, ADAM · 2010 to 2014
$40.1M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Project 3U54GM094618 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STEVENS, RAYMOND C · 2010 to 2014
$17.1M
Center for the Rational Design of Membrane Protein CrystallographyU54GM094599 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2014
$6.8M
Molecular Basis of Ang II Receptor FunctionsR01HL057470 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI KARNIK, SADASHIVA S · 1997 to 2013
$4.4M
Femtosecond nano-crystallography of membrane proteinsR01GM095583 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2023
$4.3M
TRAINING PROGRAM IN VASCULAR CELL BIOLOGYT32HL007914 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI PLOW, EDWARD FRANKLIN · 1999 to 2011
$2.2M
Regulation of AT1R-signaling and pathology in vessels through microRNAR01HL115964 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI KARNIK, SADASHIVA S · 2012 to 2015
$1.5M
HT structure determination of GPCRs by LCP serial femtosecond nanocrystallographyR01GM108635 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEREZOV, VADIM · 2014 to 2017
$1.5M
NHLBI NIH HHS HL007914NHLBI NIH HHS R01 HL057470NHLBI NIH HHS R01 HL115964NHLBI NIH HHS R01HL57470NHLBI NIH HHS T32 HL007914NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM095583NIGMS NIH HHS R01GM095583NIGMS NIH HHS R01 GM108635NIGMS NIH HHS U54 GM094586NIGMS NIH HHS U54 GM094599NIGMS NIH HHS U54 GM094618NIGMS NIH HHS U54GM094618
6 · The paper itself

Abstract

Angiotensin II type 1 receptor (AT(1)R) 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 AT(1)R blockers (ARBs), the structural basis for AT(1)R 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 AT(1)R in complex with its selective antagonist ZD7155 at 2.9-Å resolution. The AT(1)R-ZD7155 complex structure revealed key structural features of AT(1)R and critical interactions for ZD7155 binding. Docking simulations of the clinically used ARBs into the AT(1)R structure further elucidated both the common and distinct binding modes for these anti-hypertensive drugs. Our results thereby provide fundamental insights into AT(1)R structure-function relationship and structure-based drug design.

Indexed as

Amino Acid SequenceAngiotensin II Type 1 Receptor BlockersCrystallography, X-RayHumansMolecular Sequence DataMutagenesisNaphthyridinesReceptor, Angiotensin, Type 1Sequence AlignmentAGTR1 protein, humanAngiotensin II Type 1 Receptor BlockersNaphthyridinesReceptor, Angiotensin, Type 1ZD 7155

Identifiers

PMID25913193
PMCPMC4427029
OpenAlexW2110177837

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.