The Skaggs Institute for Chemical Biology
Lawrence Berkeley National Laboratory
We focus on structural biology and design projects that concern fundamental questions of molecular and cellular biology relevant to human disease. A focal point for Tainer lab research efforts is the characterization of keystone complexes, conformational changes, and interfaces for macromolecular assemblies and machines. These protein complexes relate to reactive oxygen control, genome integrity, cell proliferation, response to pathogenesis, and cell death. The goal of these ongoing characterizations is to provide a interpretation of the human health implications from the human genome polymorphisms. These structural results thus contribute to new molecular level understandings as well as to knowledge-based treatments for degenerative diseases, infectious disease, and cancer. Primarily experimental techniques include protein crystallography, electron microscopy, biochemistry, computation analyses, mutagenesis, and protein expression. Computational efforts include method developments and applications, in the areas of structural analysis, protein and drug design, and molecular computer graphics.
Ph.D., Biochemistry, Duke University, 1982
B.S., Zoology & Anthropology, Trinity College, Duke University, 1974
2013-2015 Professor of Structural Biology, Integrative Structural and Computational Biology (ISCB), The Scripps Research Institute
1982-2012 Professor of Structural Biology, Molecular Biology, The Scripps Research Institute
Hura, G.L., Menon, A.L., Hammel, M., Rambo, R.P., Poole, F.L., Tsutakawa, S.E., Jenney, F.E., Frankel, K.A., Hopkins, R.C., Scott, J.O., Dillard, B.D., Classen, S., Adams, M.W.W. and Tainer, J.A. (2009) Rapid and robust proteomics-scale solution structural analyses determined by x-ray scattering (SAXS) Nature Methods 6: 606-612. PMCID in progress.
Williams RS, Dodson GE, Limbo O, Yamada Y, Williams JS, Guenther G, Classen S, Glover JN, Iwasaki H, Russell P, Tainer JA (2009). Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. Cell 139: 87-99. PMCID: 2762657.
Tubbs JL, Latypov V, Kanugula S, Butt A, Melikishvili M, Kraehenbuehl R, Fleck O, Marriott A, Watson AJ, Verbeek B, McGown G, Thorncroft M, Santibanez-Koref MF, Millington C, Arvai AS, Kroeger MD, Peterson LA, Williams DM, Fried MG, Margison GP, Pegg AE, Tainer JA (2009) Flipping of alkylated DNA damage bridges base and nucleotide excision repair. Nature 459: 808-813. PMCID: 2729916.
Williams, RS, Moncalian, G. Williams, JS, Yamada, Y, Limbo, O, Shin, DS, Groocock, LM, Cahill, D, Hitomi, C, Guenther, G, Moiani, D, Carney, JP, Russell, P, Tainer JA (2008) Mre11 Dimers Coordinate DNA End Bridging and Nuclease Processing in Double Strand Break Repair. Cell 135: 97–109. PMCID: 268123.
Fan, L., Fuss, J.O., Cheng, Q.J., Arvai, A.S., Hammel M., Roberts, V.A., Cooper; P.K., Tainer, J.A. (2008) XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 133: 789-800.