Dr. Ching-Ju Tsai

Scientist
Paul Scherrer Institute
Forschungsstrasse 111
5232 Villigen PSI
Switzerland
Forschungsstrasse 111
5232 Villigen PSI
Switzerland
Telephone
Email
Research
G-protein coupled receptors (GPCRs) are the targets of almost half of today’s pharmaceuticals. They contribute to signal transduction across the cell membrane. GPCRs are activated by extracellular stimuli such as light, hormone, and small ligand, resulting in conformational changes and interaction with a number of signalling and regulatory proteins including G proteins, kinases and arrestins. The first step in GPCR activation leads to conformational changes which trigger interaction with G proteins. There are four main subtypes of G proteins, each inducing specific signalling pathways. Most GPCRs can couple to more than one G-protein subtype, and therefore it is fundamental to understand GPCR signalling by studying the coupling specificity between G protein and GPCRs. We aim to decipher the mechanism by which this selectivity is achieved. To do so, we use X-ray crystallography, electron cryo-microscopy (cryo-EM) together with biochemical techniques to characterize the molecular mechanism of GPCR signalling complexes.
Publications
2018
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Crystal structure of rhodopsin in complex with a mini-G o sheds light on the principles of G protein selectivity
Science Advances 4, eaat7052 (2018).DOI: 10.1126/sciadv.aat7052
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Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals
IUCRJ 5, 103 (2018).DOI: 10.1107/S2052252517017043
2017
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Structural biology Signalling under the microscope
NATURE 546, 36-37 (2017).DOI: 10.1038/nature22491
2016
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Backbone NMR reveals allosteric signal transduction networks in the beta1-adrenergic receptor
NATURE 530, 237 (2016).DOI: 10.1038/nature16577
2015
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Low-Z polymer sample supports for fixed-target serial femtosecond X-ray crystallography
JOURNAL OF APPLIED CRYSTALLOGRAPHY 48, 1072-1079 (2015).DOI: 10.1107/S1600576715010493
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Time-resolved structural studies with serial crystallography: A new light on retinal proteins
STRUCTURAL DYNAMICS 2, 041718 (2015).DOI: 10.1063/1.4922774
2014
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7 angstrom resolution in protein two-dimensional-crystal X-ray diffraction at Linac Coherent Light Source
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES 369, UNSP 20130500 (2014).DOI: 10.1098/rstb.2013.0500
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Femtosecond X-ray diffraction from two-dimensional protein crystals
IUCRJ 1, 95-100 (2014).DOI: 10.1107/S2052252514001444
2013
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Structure of beta-Adrenergic Receptors
G PROTEIN COUPLED RECEPTORS: STRUCTURE 520, 117-151 (2013).DOI: 10.1016/B978-0-12-391861-1.00006-X
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Two Alternative Conformations of a Voltage-Gated Sodium Channel
JOURNAL OF MOLECULAR BIOLOGY 425, 4074 (2013).DOI: 10.1016/j.jmb.2013.06.036