ArticleNature communications2020
DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl
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Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed.
- Comparative evaluation of noncanonical amino acids as site-specific NMR probes for the complex of E. coli SSB with single-stranded DNA without isotope labelling.The FEBS journal · 2026Article
- Functional and structural insights into interactions between β-Arrestin 1 and Gαs or Gαi1.Nature communications · 2026Article
- GPCR Phospho-Barcodes and Biased Signaling.Handbook of experimental pharmacology · 2026Review
- Conformational Heterogeneity Underlying Divergent Signaling in Class A G Protein-Coupled Receptors.ACS pharmacology & translational science · 2025Review
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors.Science (New York, N.Y.) · 2024Article
- Distinct activation mechanisms of β-arrestin-1 revealed byNature communications · 2023Article
- Crystal Structure of an Archaeal Tyrosyl-tRNA Synthetase Bound to Photocaged L-Tyrosine and Its Potential Application to Time-Resolved X-ray Crystallography.International journal of molecular sciences · 2022Article
- Progesterone activates GPR126 to promote breast cancer development via the Gi pathway.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- QR code model: a new possibility for GPCR phosphorylation recognition.Cell communication and signaling : CCS · 2022Review
- Site-specific DNA functionalization through the tetrazene-forming reaction in ionic liquids.Chemical science · 2022Article
- Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR.Nature communications · 2021Article
- Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Evaluation of the tert-butyl group as a probe for NMR studies of macromolecular complexes.Journal of biomolecular NMR · 2021Article
- Activation pathway of a G protein-coupled receptor uncovers conformational intermediates as targets for allosteric drug design.Nature communications · 2021Article
- Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2.Nature communications · 2021Article
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Authors and funding
33 authors.
Qi Liu *Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Qing-Tao He *Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Xiaoxuan Lyu *Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Fan Yang *Key Laboratory Experimental Teratology of the Ministry of Education and Department of Physiology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, Shandong, 250012, China.
Zhong-Liang Zhu *School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui, 230026, China.
Peng XiaoKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, 250012, Shandong, China.
Zhao YangKey Laboratory Experimental Teratology of the Ministry of Education and Department of Physiology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, Shandong, 250012, China.
Feng ZhangInstitute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Zhao-Ya YangInstitute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Xiao-Yan WangInstitute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Peng SunWuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, 30 Xiaohongshan Road, Wuchang District, Wuhan, Hubei, 430071, China.
Qian-Wen WangWuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, 30 Xiaohongshan Road, Wuchang District, Wuhan, Hubei, 430071, China.
Chang-Xiu QuKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, 250012, Shandong, China.
Zheng GongKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, 250012, Shandong, China.
Jing-Yu LinKey Laboratory Experimental Teratology of the Ministry of Education and Department of Physiology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, Shandong, 250012, China.
Zhen XuInstitute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Shao-le SongInstitute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Shen-Ming HuangKey Laboratory of Molecular Cardiovascular Science, Ministry of Education, Peking University, 15 Xueyuan Road, Haidian District, Beijing, 100191, China.
Sheng-Chao GuoKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, 250012, Shandong, China.
Ming-Jie HanInstitute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.ORCID http://orcid.org/0000-0001-5065-705X
Kong-Kai ZhuSchool of Biological Science and Technology, University of Jinan, 336 Nanxinzhuangxi Road, Shizhong District, Jinan, 250022, China.
Xin ChenDepartment of Medicinal Chemistry, School of Pharmaceutical Engineering and Life Science, Changzhou University, Changzhou, Jiangsu, 213164, China.
Alem W KahsaiDuke University, School of Medicine, Durham, NC, 27705, USA.
Kun-Hong XiaoDepartment of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA, 15261, USA.
Wei KongKey Laboratory of Molecular Cardiovascular Science, Ministry of Education, Peking University, 15 Xueyuan Road, Haidian District, Beijing, 100191, China.ORCID http://orcid.org/0000-0001-6720-6810
Fa-Hui LiInstitute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China.
Ke RuanHefei National Laboratory for Physical Science at the Microscale, University of Science and Technology of China, 443 Huangshan Road, Hefei, Anhui, 230027, China.ORCID http://orcid.org/0000-0001-9358-0451
Zi-Jian LiKey Laboratory of Molecular Cardiovascular Science, Ministry of Education, Peking University, 15 Xueyuan Road, Haidian District, Beijing, 100191, China.
Xiao YuKey Laboratory Experimental Teratology of the Ministry of Education and Department of Physiology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, Shandong, 250012, China.
Xiao-Gang NiuBeijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, School of Life Sciences, Peking University, Beijing, 100084, China.
Chang-Wen JinBeijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, School of Life Sciences, Peking University, Beijing, 100084, China.
Jiangyun WangInstitute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing, 100101, China. jwang@ibp.ac.cn.
Jin-Peng SunKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University, 44 Wenhua Xi Road, Jinan, 250012, Shandong, China. sunjinpeng@sdu.edu.cn.ORCID http://orcid.org/0000-0003-3572-1580
Funding
No grant is acknowledged in the PubMed record.
Abstract
Characterization of the dynamic conformational changes in membrane protein signaling complexes by nuclear magnetic resonance (NMR) spectroscopy remains challenging. Here we report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, through genetic code expansion. Crystallographic analysis revealed structural changes that reshaped the TMSiPhe-specific amino-acyl tRNA synthetase active site to selectively accommodate the trimethylsilyl (TMSi) group. The unique up-field
Indexed as
LigandsArrestinbeta-Arrestin 1Binding SitesCrystallography, X-RayHumansModels, MolecularPhenylalanineProtein BindingProtein ConformationProton Magnetic Resonance SpectroscopyReceptors, Adrenergic, beta-2Signal TransductionARRB1 protein, humanArrestinbeta-Arrestin 1LigandsPhenylalanineReceptors, Adrenergic, beta-2
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