Christopher G. Tate

Christopher G. Tate (born 5 May 1964) is an English membrane protein biochemist and molecular biologist who works at the Medical Research Council Laboratory of Molecular Biology in Cambridge, UK. Tate is known for his contributions to the understanding of G protein-coupled receptors.[1]

Christopher G. Tate
Born (1964-05-05) 5 May 1964
NationalityBritish
Alma materUniversity of Bristol (BSc (Hons), PhD)
Scientific career
Fieldsmembrane protein biochemist and molecular biologist
InstitutionsLaboratory of Molecular Biology (LMB)
Doctoral advisorMichael J. A. Tanner
Websitehttps://www2.mrc-lmb.cam.ac.uk/group-leaders/t-to-z/chris-tate/

Education

Tate was awarded the degree of BSC (Hons) in biochemistry by the University of Bristol in 1985. He was then awarded a PhD in 1989 by the University of Bristol for his work on integral membrane proteins in the red blood cell, under the supervision of Michael J. A. Tanner.[1]

Career and research

Tate worked as a postdoctoral researcher (1989–1992) at the Department of Biochemistry, Cambridge, on bacterial sugar transporters in the group of Peter J. F. Henderson. After obtaining a research fellowship at Girton College, Cambridge, he then moved in 1992 to the Medical Research CoUncil Laboratory of Molecular Biology to work with Richard Henderson, initially on the serotonin transporter and then on the structure determination of the multidrug EmrE transporter[2] by electron crystallography. Whilst working in Henderson's group, Tate developed the method of conformational thermostabilisation[3] of G protein-coupled receptors. This allowed the structure determination of the beta1-adrenoceptor[4] in collaboration with the group of Gebhard F.X. Schertler. The methodology was patented[5] and used as the basis for the foundation of the drug discovery company Heptares Therapeutics Ltd[6] (HTL) in July 2007 by Tate, Henderson, Fiona Marshall (CSO) and Malcolm Weir (CEO).

Tate became an independent group leader in 2010 and since then his group has used structural biology to discover how the beta1-adrenoceptor[7] and the adenosine A2A receptor[8] are activated. In collaboration with the group of Reinhard Grisshammer (NIH, Bethesda), the structure of the thermostabilised neurotensin receptor was determined[9] bound to a peptide agonist. Recent work has focused on understanding how G proteins coupled to G protein-coupled receptors,[10][11] which has been facilitated by the development of mini-G proteins.[12]

References
  2. Ubarretxena-Belandia, Iban; Baldwin, Joyce M.; Schuldiner, Shimon; Tate, Christopher G. (2003). "Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer". The EMBO Journal. 22 (23): 6175–6181. doi:10.1093/emboj/cdg611. ISSN 0261-4189. PMC 291852. PMID 14633977.
  3. Serrano-Vega, Maria J.; Magnani, Francesca; Shibata, Yoko; Tate, Christopher G. (2008). "Conformational thermostabilization of the beta1-adrenergic receptor in a detergent-resistant form". Proceedings of the National Academy of Sciences of the United States of America. 105 (3): 877–882. Bibcode:2008PNAS..105..877S. doi:10.1073/pnas.0711253105. ISSN 1091-6490. PMC 2242685. PMID 18192400.
  4. Warne, Tony; Serrano-Vega, Maria J.; Baker, Jillian G.; Moukhametzianov, Rouslan; Edwards, Patricia C.; Henderson, Richard; Leslie, Andrew G. W.; Tate, Christopher G.; Schertler, Gebhard F. X. (2008). "Structure of a beta1-adrenergic G-protein-coupled receptor". Nature. 454 (7203): 486–491. Bibcode:2008Natur.454..486W. doi:10.1038/nature07101. ISSN 1476-4687. PMC 2923055. PMID 18594507.
  5. "World Intellectual Property Organization".
  6. "Heptares Ltd". Archived from the original on 2018-08-26. Retrieved 2018-08-20.
  7. Warne, Tony; Moukhametzianov, Rouslan; Baker, Jillian G.; Nehmé, Rony; Edwards, Patricia C.; Leslie, Andrew G. W.; Schertler, Gebhard F. X.; Tate, Christopher G. (2011). "The structural basis for agonist and partial agonist action on a β(1)-adrenergic receptor". Nature. 469 (7329): 241–244. Bibcode:2011Natur.469..241W. doi:10.1038/nature09746. ISSN 1476-4687. PMC 3023143. PMID 21228877.
  8. Lebon, Guillaume; Warne, Tony; Edwards, Patricia C.; Bennett, Kirstie; Langmead, Christopher J.; Leslie, Andrew G. W.; Tate, Christopher G. (2011). "Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation". Nature. 474 (7352): 521–525. doi:10.1038/nature10136. ISSN 1476-4687. PMC 3146096. PMID 21593763.
  9. White, Jim F.; Noinaj, Nicholas; Shibata, Yoko; Love, James; Kloss, Brian; Xu, Feng; Gvozdenovic-Jeremic, Jelena; Shah, Priyanka; Shiloach, Joseph (2012). "Structure of the agonist-bound neurotensin receptor". Nature. 490 (7421): 508–513. Bibcode:2012Natur.490..508W. doi:10.1038/nature11558. ISSN 1476-4687. PMC 3482300. PMID 23051748.
  10. García-Nafría, Javier; Nehmé, Rony; Edwards, Patricia C.; Tate, Christopher G. (2018). "Cryo-EM structure of the serotonin 5-HT1B receptor coupled to heterotrimeric Go". Nature. 558 (7711): 620–623. Bibcode:2018Natur.558..620G. doi:10.1038/s41586-018-0241-9. ISSN 1476-4687. PMC 6027989. PMID 29925951.
  11. Carpenter, Byron; Nehmé, Rony; Warne, Tony; Leslie, Andrew G. W.; Tate, Christopher G. (2016). "Structure of the adenosine A(2A) receptor bound to an engineered G protein". Nature. 536 (7614): 104–107. Bibcode:2016Natur.536..104C. doi:10.1038/nature18966. ISSN 1476-4687. PMC 4979997. PMID 27462812.
  12. Carpenter, Byron; Tate, Christopher G. (2016). "Engineering a minimal G protein to facilitate crystallisation of G protein-coupled receptors in their active conformation". Protein Engineering, Design & Selection: PEDS. 29 (12): 583–594. doi:10.1093/protein/gzw049. ISSN 1741-0134. PMC 5181381. PMID 27672048.
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