Jon Clardy
Chemist who solved the crystal structure of the FKBP12-rapamycin-FRB (mTOR) complex, showing how rapamycin acts as a molecular glue between two proteins.
Professor of Biological Chemistry and Molecular Pharmacology, Harvard Medical School (since 2002) · Cornell University (1978–2002)
Portrait: Harvard Medical School
Jon Clardy is a chemist who studies small molecules made by bacteria and fungi and how they control biological processes. He earned his PhD in chemistry at Harvard in 1969, taught at Iowa State and then at Cornell from 1978 to 2002, and joined Harvard Medical School in 2002.
With Stuart Schreiber he determined the crystal structures of the immunosuppressant drugs FK506 and rapamycin bound to FKBP12. He is also a co-founder of Harvard's chemical biology PhD program.
The 1996 study in this Atlas, from his Cornell lab, showed the structure of FKBP12 and rapamycin bound to the FRB domain of mTOR (then called FRAP). Rapamycin sits in two pockets at once and glues the two proteins together. It became a textbook example of a small molecule that brings two proteins into contact.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 1996 | M | Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP CHO1996 Crystal structure at 2.7 angstroms of FKBP12-rapamycin bound to the FRB domain of human FRAP/mTOR, showing rapamycin as a molecular glue; Clardy is the senior (last) author. |
Co-authors in the Atlas 1
People with a profile here who share at least one study with Jon Clardy.
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- Stuart L. Schreiber Co-discovered mTOR in 1994 (his group called it FRAP) as the mammalian target of the FKBP12–rapamycin complex, and helped found chemical biology as a field
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