Complexes of the neurotensin receptor 1 with small-molecule ligands reveal structural determinants of full, partial, and inverse agonism.

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作者： Mattia,Deluigi ^[1] ; Alexander,Klipp ^[1] ; Christoph,Klenk ^[1] ; Lisa,Merklinger ^[1] ; Stefanie A,Eberle ^[1] ; Lena,Morstein ^[1] ; Philipp,Heine ^[1] ; Peer R E,Mittl ^[1] ; Patrick,Ernst ^[1] ; Theodore M,Kamenecka ^[2] ; Yuanjun,He ^[2] ; Santiago,Vacca ^[1] ; Pascal,Egloff ^[1] ; Annemarie,Honegger ^[1] ; Andreas,Plückthun ^[3]

作者单位： Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland. ^[1] Department of Molecular Medicine, The Scripps Research Institute, Scripps Florida, 130 Scripps Way #A2A, Jupiter, FL 33458, USA. ^[2] Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland. plueckthun@bioc.uzh.ch. ^[3]

DOI 10.1126/sciadv.abe5504

PMID 33571132

发布时间 2022-04-18

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Science advances

2021年7卷5期

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Complexes of the neurotensin receptor 1 with small-molecule ligands reveal structural determinants of full, partial, and inverse agonism.

Science advances

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Complexes of the neurotensin receptor 1 with small-molecule ligands reveal structural determinants of full, partial, and inverse agonism.

Science advances

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Science advances

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