- Assistant Professor, Structural Biology Initiative
- Assistant Professor of Chemistry & Biochemistry, The City College of New York
Daniel Keedy, Ph.D.
Prior to his appointment, Daniel Keedy, Ph.D. was an AP Giannini Postdoctoral Fellow in Bioengineering and Therapeutic Sciences at the University of California, San Francisco working with Professor James Fraser. He earned his PhD in Biochemistry and Structural Biology & Biophysics from Duke University working with Jane and David Richardson, after receiving his BA in Biochemistry & Molecular Biology from Rhodes College. His research on protein structural flexibility, temperature-dependent X-ray crystallography, and allosteric regulation has led to over 15 publications in leading scientific journals and over ten presentations at a variety of scientific meetings.
Professor Keedy was appointed to the ASRC in January 2018.
About the Keedy Lab
The Keedy Lab combines computation and experiments to reveal alternative protein conformations and explore how they underlie dynamic functions such as catalysis, ligand binding, and allosteric regulation.
Research Interests
Professor Keedy develops experimental and computational methods to control proteins by biasing toward specific conformations that underlie functions such as allostery, ligand binding, and catalysis. His work reveals new opportunities to modulate the activities of therapeutic targets such as tyrosine phosphatases with small molecules and protein engineering, and also offers insights into more general evolutionary processes that led to functional diversity in the human genome.
Publications
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Mehlman T. S., Biel J. T., Azeem S. M., Nelson E. R., Hossain S., Dunnett L., Paterson N. G., Douangamath A., Talon R., Axford D., Orins H., von Delft F., Keedy D. A. Room-temperature crystallography reveals altered binding of small-molecule fragments to PTP1B. eLife 2023 12:e84632 |
A Ebrahim*, BT Riley*, D Kumaran, B Andi, MR Fuchs, S McSweeney, DA Keedy (* contributed equally). “The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (Mpro).” Accepted to IUCrJ (2022). Also available as a bioRxiv preprint (2021) |
Riley BT, Wankowicz SA, de Oliveira SHP, van Zundert GCP, Hogan DW, Fraser JS, Keedy DA*, van den Bedem H* (* co-corresponding authors). qFit 3: Protein and ligand multiconformer modeling for X-ray crystallographic and single-particle cryo-EM density maps. Protein Science, 2021, Volume 30, Issue 1. |
D.A. Keedy. Journey to the center of the protein: allostery from multitemperature multiconformer X-ray crystallography. Acta Cryst D, 2019, 75:123-137. PMID: 30821702. |
D.A. Keedy, Z.B. Hill, J.T. Biel, E. Kang, T.J. Rettenmaier, J. Brandao-Neto, N.M. Pearce, F. von Delft, J.A. Wells, J.S. Fraser. An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering. eLife, 2018. DOI: 10.7554/eLife.36307. |
