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Scientist at The Scripps Research Institute Elected to Royal Society

La Jolla, CA. May 25, 2000 -- Ian A. Wilson, D.Phil., Professor, Department of Molecular Biology and The Skaggs Institute for Chemical Biology at The Scripps Research Institute (TSRI), has been elected to fellowship in the Royal Society, the independent scientific academy of the United Kingdom, dedicated to promoting excellence in science. Founded in 1660, the Royal Society's objectives are to recognize excellence in science; support leading-edge scientific research and its applications; stimulate international interactions; further the role of science, engineering and technology in society; and promote the public's understanding of science.

Wilson has been invited to participate in Admissions Day in London on Friday, July 14, 2000, preceded by a New Fellows Seminar, July 12-13.

An internationally recognized scientist known principally for his work in the field of x-ray crystallography, he received a B.Sc. in biochemistry from the University of Edinburgh and a D.Phil., in molecular biophysics from Oxford University, England. After completing a postdoctoral fellowship in biochemistry and teaching assignments at Harvard University, Wilson joined TSRI's faculty in the Department of Immunology in 1982. In 1991, he became a professor in the Department of Molecular Biology and in 1996, he was named to a professorship in The Skaggs Institute for Chemical Biology. He is a member of the faculty of the Graduate Program at TSRI and also became an adjunct professor in the Department of Pathology at University of California, San Diego, in 1998.

Wilson's research has led to significant advances in the scientific understanding of molecular recognition in the immune system and in signal transduction by cytokine hormone receptors. Through his efforts, breakthroughs have been achieved in several areas of structural biology, immunology, chemistry, biology, and biochemistry, particularly in understanding the chemistry of antibody-antigen recognition, the mechanism of catalytic antibodies, cellular-immune recognition by T cell receptor-MHC interaction, the mechanism of growth hormone-cytokine receptor signaling, and the identification and mechanisms of novel small molecule mimetics of natural hormones.

One of his most notable achievements was the determination of the three-dimensional structure of the T cell receptor, a key component of the immune response. Called "the holy grail for cellular immunologists," many laboratories throughout the world had been attempting to crystallize the TCR molecule without success. Four years ago, Wilson's discovery caused Science magazine to cite it as the runner-up for the Science "Breakthrough of the Year." Understanding the structure of the TCR and its function may enable scientists to enhance the effectiveness of the immune system through the development of new, highly targeted therapeutics. According to TSRI President Richard A. Lerner, "This was one of the most important structures to be elucidated in the past decade."

In addition, his research group was the first to provide evidence that small peptides can mimic large protein hormones, an achievement that earned Wilson the Newcomb-Cleveland Award for an outstanding contribution to science by the American Association for the Advancement of Science and Science magazine. They not only identified a peptide that binds and activates the receptor for erythropoietin (EPO) a hormone that controls red blood cell production but found that it binds to a similar site as the natural hormone. These studies have broad implications for the production and method of administration of erythropoietin, the largest single product in biotechnology whose recombinant form is widely used in the treatment of patients with anemia caused by renal failure, cancer chemotherapy and AZT treatment. Currently available by injection only, this work may contribute to the possibility of designing orally active drugs that could promote the growth of red blood cells.

Recently he has turned his attention to a study of folate-dependent enzymes in purine biosynthesis. Inhibition of these enzymes has reduced solid tumors in animal models and humans. Wilson's work has revealed how inhibition of conformational changes in the binding site could lead to new avenues to find novel, non-folate, anti-neoplastic drugs.

Wilson is a member of numerous professional societies, including the British Biophysical Society, American Society of Virologists, American Association of Pathologists, American Crystallographic Association, British Society of Immunologists, Protein Society, and American Chemical Society. He currently serves on the Board of Reviewing Editors of Science and as associate editor of the Journal of Molecular Biology, Immunity, and the Journal of Experimental Medicine.

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