Raymond C. Stevens (born 1963) is an American chemist and structural biologist, Founder, CEO and Board Member of Structure Therapeutics;https://structuretx.com/ Founding Director of the at ShanghaiTech University; Professor Emeritus of Chemistry, and Founding Director of the Bridge Institute at the University of Southern California; Board Member, Danaher Corporation.
Biography Stevens was born into a military family. In 1969 his father died in the Air Force, and his mother took several part-time jobs to support the family. He was raised in Auburn, Maine.
In 1980, Stevens joined the Army under their split option training program and conducted basic training at Fort Dix, New Jersey and advanced individual training at Fort Sam Houston, Texas. While engaged in his military service, Stevens entered the University of Southern Maine in the Computer Science program in 1981. However, an enthusiastic professor (John Ricci) converted him to the study of Chemistry. He spent two summers working as an intern at the Brookhaven National Laboratory in Long Island with Professor Ricci, and Drs. Thomas Koetzle and Dick McMullan, where he first learned how to determine the molecular structure of compounds by X-ray and neutron diffraction. While there he also met a University of Southern California research team led by Dr. Robert Bau; after he obtained a Bachelor of Science degree in chemistry at USM, he entered the University of Southern California in pursuit of a Doctor of Philosophy degree in Chemistry working with Professor Robert Bau and Nobel Laureate Professor, George Olah. He completed his Ph.D. in 26 months, graduating in 1988.
Although science is a major part of his life, Stevens climbs mountains with his wife and children and runs ultramarathons including the Vermont 100 Mile Endurance RunVermont100 race results 2006 and American River 50 Mile Endurance Run,American River 50 Miler race results and in 2011 he successfully completed the 156 mile Marathon des Sables across the Moroccan Sahara Desert. Currently working on climbing the 7 highest mountains on the 7 continents, he has climbed Mt. Kilimanjaro, Mt. Elbrus, Aconcagua, Vinson Massif and Mt. Kosciuszko. Next mountains are Mt. Everest and Denali.
Scientific career After obtaining his Ph.D., Stevens accepted a postdoctoral position in 1988 in the lab of Nobel Laureate William N. Lipscomb, Jr. in the chemistry department at Harvard University where he focused on the large allosteric enzyme aspartate carbamoyltransferase.Stevens, R. C., & Lipscomb, W. N., "Allosteric Enzymes" Eds., R. Diamond, T. F. Koetzle, K. Prout, & J. Richardson, Molecular Structures in Biology (Oxford, UK: Oxford University Press, 1993) pp. 223–259.Stebbins, J. W., Robertson, D. E., Roberts, M. F., Stevens, R. C., Lipscomb, W. N., & Kantrowitz, E. R., "Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR, and X-ray crystallographic study," Prot. Sci. 1, 1435–1446 (1992).Stevens, R. C., & Lipscomb, W. N., "A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamylase," Proc. Natl. Acad. Sci. USA 89, 5281–5285 (1992).Stevens, R. C., Reinisch, K. M., & Lipscomb, W. N., "Molecular Structure of Bacillus subtilis Aspartate transcarbamoylase at 3.0 A Resolution," Proc. Natl. Acad. Sci. USA 88, 6087–6091 (1991).Stevens, R. C., Chook, Y. M., Cho, C. Y., Lipscomb, W. N., & Kantrowitz, E. R., "Escherichia coli aspartate carbamoyltransferase: The probing of crystal structure analysis via site-specific mutagenesis," Protein Engineering 4, 391–408 (1991).Gouaux, J. E., Stevens, R. C., & Lipscomb, W. N., "Crystal Structures of Aspartate Carbamoyltransferase Li gated with Phosphonoacetamide, Malonate and CTP or ATP at 2.8-A Resolution and Neutral pH," Biochemistry 29, 7702–7715 (1990).Stevens, R. C., J.E. Gouaux, & Lipscomb, W. N., "Structural Consequences of Effector Binding to the T State of Aspartate Carbamoyltransferase Crystal Structures of the Unligated and ATP- and CTP-Complexed Enzymes at 2.6-A Resolution," Biochemistry 29, 7691–7701 (1990).Stevens, R. C., & Lipscomb, W. N., "Allosteric control of quaternary states in E. coli aspartate transcarbamylase," Biochemistry and Biophysics Research Communications 171, 1312–1318 (1990).Gouaux, J. E., Stevens, R. C., Ke, H., & Lipscomb, W. N., "Crystal structure of the Glu-239 to Gln mutant of aspartate carbamoyltransferase at 3.1 A resolution: An intermediate quaternary structure," Proc. Natl. Acad. Sci. USA 86, 8212–8216 (1989). In 1991, he accepted a tenure-track position at the University of California, Berkeley in the chemistry department with a joint appointment in neurobiology. His initial research as an assistant professor focused on structural neurobiology and immunology, combining chemistry, structural biology and protein chemistry with a specific biological interest in understanding how the G protein-coupled receptor (GPCR) superfamily works. A seminal collaboration for Stevens was with Professor Peter G. Schultz where they jointly published a series of Science and Nature papers describing the immunological evolution of antibodies through careful structural studies.H. D. Ulrich, E. Mundorff, B. D. Santarsiero, E. M. Driggers, R. C. Stevens and P. G. Schultz (1997) The interplay between binding energy and catalysis in the evolution of a catalytic antibody Nature 389: 271–5G. J. Wedemayer, P. A. Patten, L. H. Wang, P. G. Schultz and R. C. Stevens (1997) Structural insights into the evolution of an antibody combining site Science 276: 1665–9F. E. Romesberg, B. Spiller, P. G. Schultz and R. C. Stevens (1998) Immunological origins of binding and catalysis in a Diels-Alderase antibody Science 279: 1929–33A. Simeonov, M. Matsushita, E. A. Juban, E. H. Thompson, T. Z. Hoffman, A. E. t. Beuscher, M. J. Taylor, P. Wirsching, W. Rettig, J. K. McCusker, R. C. Stevens, D. P. Millar, P. G. Schultz, R. A. Lerner and K. D. Janda (2000) Blue-fluorescent antibodies Science 290: 307–13 In 1999, Stevens left Berkeley to take a tenured position at The Scripps Research Institute. While at The Scripps Research Institute, Stevens has helped to found and establish the Joint Center for Structural Genomics,www.jcsg.org Joint Center for Innovative Membrane Protein Technologies,jcimpt.scripps.edu and the GPCR Network,cmpd.scripps.edu all funded by the National Institutes of Health with direct guidance from NIGMS. In 2012, Stevens co-founded the at ShanghaiTech University.ihuman.shanghaitech.edu.cn In 2014, Stevens moved his lab from The Scripps Research Institute to the University of Southern California, where he is currently the Provost Professor of Biological Sciences and Chemistry and he founded the Bridge Institute to converge the arts and sciences.
Stevens is known for obtaining the structures of many biologically significant proteins and his technological innovations. He is considered a pioneer of high-throughput x-ray crystallography and structural genomics.R. C. Stevens and I. A. Wilson (2001) Tech.Sight. Industrializing structural biology. Science 293: 519-20 His laboratory has led to the contribution of over 500 protein structure entries in the Protein Data Bank www.pdb.org. Stevens has withdrawn two different structures of ligand-bound clostridial neurotoxins.M. A. Hanson, R. C. Stevens (2009) Retraction: Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution Nat Struct Mol Biol. 16(7):795.M. A. Hanson, T. K. Oost, C. Sukonpan, D. H. Rich, R. C. Stevens (2002) Structural Basis for BABIM Inhibition of Botulinum Neurotoxin Type B Protease [J. Am. Chem. Soc. 2000, 122, 11268−11269] J. Am. Chem. Soc. 124(34):10248–10248
In October 2007, Stevens and colleagues published the first high-resolution structure of a human GPCR.USC College : News : October 2007 : Raymond StevensV. Cherezov, D. M. Rosenbaum, M. A. Hanson, S. G. Rasmussen, F. S. Thian, T. S. Kobilka, H. J. Choi, P. Kuhn, W. I. Weis, B. K. Kobilka and R. C. Stevens (2007) High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor Science 318: 1258–65. The β2-adrenergic receptor work was quickly followed up 9 months later by the determination of the structure of the human A2A adenosine receptor structure,V. P. Jaakola, M. T. Griffith, M. A. Hanson, V. Cherezov, E. Y. Chien, J. R. Lane, A. P. Ijzerman and R. C. Stevens (2008) The 2.6 Angstrom Crystal Structure of a Human A2A Adenosine Receptor Bound to an Antagonist, Science 322: 1211–7 also known as the caffeine receptor. In 2010, the structures of the human chemokine CXCR4 receptor (HIV co-receptor),B. Wu, E.Y.T. Chien, C.D. Mol, G. Fenalti, W. Liu, V. Katritch, R. Abagyan, A. Brooun, P. Wells, F.C. Bi, D.J. Hamel, P. Kuhn, T.M. Handel, V. Cherezov, R.C. Stevens "Structures of the CXCR4 chemokine GPCR with small molecule and cyclic peptide antagonists" Science 330, 1066-1071 (2010). the human dopamine D3 receptorE.Y.T. Chien, W. Liu, Q. Zhao, V. Katritch, G.W. Han, M.A. Hanson, L. Shi, A.H. Newman, J.A. Javitch, V. Cherezov, R.C. Stevens "Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist" Science 330, 1091-1095 (2010). and the human Histamine H1 receptorT. Shimamura, M. Shiroishi, S. Weyand, H. Tsujimoto, G. Winter, V. Katritch, R. Abagyan, V. Cherezov, W. Liu, G.W. Han, T. Kobayashi, R.C. Stevens, S. Iwata. "Structure of the human histamine H1 receptor in complex with doxepin" Nature 475, 65-70 (2011). were published. In addition to these inactive-state structures, Stevens and colleagues solved the structure of an agonist-bound A2A adenosine receptor.F. Xu, H. Wu, V. Katritch, G.W. Han, K.A. Jacobson, Z.-G. Gao, V. Cherezov, R.C. Stevens "Structure of an agonist-bound human A2A adenosine receptor" Science 332, 322-327 (2011).
Subsequent novel human receptor structures include:
2012: The first structure of a lipid-activated GPCR, the sphingolipid,M. A. Hanson, C. B. Roth, E. Jo, M. T. Griffith, F. L. Scott, G. Reinhart, H. Desale, B. Clemons, S. M. Cahalan, S. C. Schuerer, M. G. Sanna, G. W. Han, P. Kuhn, H. Rosen and R. C. Stevens (2012) Crystal structure of a lipid G protein-coupled receptor Science 335: 851-5 the human kappa-opioid receptorH. Wu, D. Wacker, M. Mileni, V. Katritch, G. W. Han, E. Vardy, W. Liu, A. A. Thompson, X. P. Huang, F. I. Carroll, S. W. Mascarella, R. B. Westkaemper, P. D. Mosier, B. L. Roth, V. Cherezov and R. C. Stevens (2012) Structure of the human kappa-opioid receptor in complex with JDTic Nature 485: 327-332 and the human nociceptin/orphanin FQ peptide receptor.A. A. Thompson, W. Liu, E. Chun, V. Katritch, H. Wu, E. Vardy, X. P. Huang, C. Trapella, R. Guerrini, G. Calo, B. L. Roth, V. Cherezov and R. C. Stevens (2012) Structure of the nociceptin/orphanin FQ receptor in complex with a peptide mimetic Nature 485: 395-9