Dr. Kobilka is the Hélène Irwin Fagan Chair in Cardiology and a Professor in the Department of Molecular and Cellular Physiology at Stanford University. He is a co-recipient of the 2012 Nobel Prize in Chemistry (together with his postdoctoral mentor, Prof. Robert Lefkowitz) for their studies of G protein-coupled receptors.
Trained initially as a physician at the Yale University School of Medicine, Dr. Kobilka was a cardiology fellow at Duke University with Prof. Robert Lefkowitz. At Duke, Dr. Kobilka and his colleagues were the first to identify, purify, and clone a series of genes that encoded mammalian adrenergic receptors. It was then realized that these receptors were similar in topology to the light-sensitive photoreceptor in the eye, rhodopsin, and that an entire family of such receptors exists: the G protein-coupled receptors (GPCRs). Today, this class of receptors is recognized as the largest family of transmembrane receptors in humans, containing over 800 members. Approximately one-third of all commercially available drugs use GPCRs as targets.
At Stanford University, Prof. Kobilka embarked on a journey to determine the first high-resolution crystal structure of a ligand-binding GPCR, the beta-2 adrenergic receptor. Soon after this elusive protein structure was published in 2007 (1), Prof. Kobilka’s team also determined the crystal structure of the first GPCR-G protein complex (2), which, for the first time, revealed the molecular details of GPCR signaling in action. This groundbreaking discovery and the associated protein and nanobody engineering methodology paved the way for many more structures of GPCRs and GPCR-G protein complexes to be determined by X-ray crystallography and, more recently, by cryo-electron microscopy.
Prof. Kobilka is a quintessential interdisciplinary scientist. In addition to his efforts in cell and molecular biology, biochemistry, and structural biology, Prof. Kobilka has applied many biophysical techniques to study the mechanisms of GPCR signaling. These techniques include double electron-electron resonance spectroscopy, NMR spectroscopy, atomic force microscopy, molecular dynamics simulations, and single-molecule FRET microscopy. Current efforts in Prof. Kobilka’s laboratory are focused on using a series of structural and biophysical tools to elucidate the dynamic structures of GPCRs and investigate the influence of pharmacological agents on GPCR signaling.
In addition to his scientific achievements, Prof. Kobilka is a devoted advocate for physician-scientists. He has played an important role in integrating scientific research in the medical training curriculum at the Stanford University School of Medicine. Prof. Kobilka is also the vice-president of the Physician-Scientist Support Foundation, a group of researchers who share a passion for encouraging the training of biomedical researchers and continuing the advancement of physician-scientist research efforts.
1) Rasmussen, S. G. F., Choi, H., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., Burghammer, M., Ratnala, V. R. P., Sanishvili, R., Fischetti, R. F., Schertler, G. F. X., Weis, W. I. & Kobilka, B. K. Crystal structure of the human beta-2 adrenergic G-protein-coupled receptor. Nature 450, 383–388 (2007).
2) Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., Mathiesen, J. M., Shah, S. T. A., Lyons, J. A., Caffrey, M., Gellman, S. H., Steyaert, J., Skiniotis, G., Weis, W. I., Sunahara, R. K. & Kobilka, B. K. Crystal structure of the β2Adrenergic receptor-Gs protein complex. Nature 477, 549–555 (2011).
About the John T. Edsall Lecture
The Edsall Lecture is given annually in honor of John Edsall, a member of the faculty of Harvard University from 1928 to 1973, when he became emeritus but remained engaged in research for more than 20 years. He died in 2002 a few months short of 100 years of age. Dr. Edsall’s scientific career started in Edwin J. Cohn’s Department of Physical Chemistry at Harvard Medical School, where he studied the properties of the muscle proteins and of the amino acids. These studies among many others led to the 1943 book by Cohn and Edsall, Proteins, Amino Acids and Peptides as Ions and Dipolar Ions, which became a classic in the field of protein chemistry. During World War II he had a key role in isolating blood proteins for the war effort and developed fibrin foam, a porous form of a fibrin clot for use in neurosurgical procedures. In 1954, Dr. Edsall joined the Faculty of Arts and Sciences and moved to the Biological Laboratories, where he started research on carbonic anhydrase. He was greatly concerned with education. He was a tutor in the biochemical sciences concentration for 40 years and Head Tutor from more than 25 years. He taught a course on biophysical chemistry at the college from 1940 until he retired; the course led to the writing of a textbook with his closest scientific colleague, Jeffries Wyman. He had a leading role in 1954 in the formation of the Committee on Higher Degrees in Biochemistry, a graduate program leading to the PhD degree in biochemistry; the committee became the Department of Biochemistry and Molecular Biology in 1967. Dr. Edsall was also a champion in the fight for the freedom and integrity of science.