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C. Denise Okafor

Assistant Professor of Biochemistry and Molecular Biology, and of Chemistry
Denise Okafor

About Me

Denise Okafor received her B.S. in biomedical chemistry from Oral Roberts University. She earned an M.S. in chemistry and a Ph.D. in biochemistry at Georgia Institute of Technology. Her dissertation research was focused on the metallobiochemistry of RNA, investigating RNA folding and function as mediated by divalent cations magnesium and iron. Her postdoctoral research in the Ortlund lab at Emory University was focused on nuclear receptors, a family of ligand-regulated transcription factors. She used molecular dynamics simulations to investigate the mechanisms underlying ligand activation in nuclear receptors. As an NIH-IRACDA postdoctoral fellow, Denise also taught at Morehouse and Spelman colleges in Atlanta. 


Program or Departmental Affiliations

BMMB Graduate Program The Department of Chemistry



Research Summary

We investigate structural mechanisms of signaling and regulation in protein complexes. We use MD simulations to determine how conformational dynamics of proteins are altered in different functional states. A broad range of biochemical and structural techniques are also employed. Combined, these allow us to carefully elucidate molecular mechanisms that govern the regulation of protein function. By understanding how proteins are regulated endogenously, we aim to identify novel strategies to selectively modulate protein function. Nuclear receptors are one of our favorite classes of molecules to study, because of the fascinatingly complex but elegant allosteric regulatory mechanisms that drive their function. They also play critical roles in metabolism, development, reproduction and other biological processes, which make them highly attractive therapeutic targets.



Honors and Awards

  • Keystone Symposia Fellow, 2019-2020
  • Burroughs Wellcome Fund Career Award at the Scientific Interface, 2018-2023
  • Ford Foundation Postdoctoral Fellowship, 2018 (declined)
  • Protein Society Hans Neurath Outstanding promise Travel Award, 2018
  • NIH-IRACDA Postdoctoral Fellow, 2015-2018



Selected Publications

  • Okafor, C.D.; Hercules, D.; Kell, S.A.; and Ortlund E.A. Rewiring ancient residue interaction networks drove the evolution of specificity in steroid receptors. Structure 2020 (in press).
  • Okafor, C.D.; Colucci, J.K.; and Ortlund E.A. Ligand-Induced Allosteric Effects Governing SR Signaling. Nuclear Receptor Research 2019, 6.
  • Frank, F.F.; Okafor, C.D.; and Ortlund E.A. The first crystal structure of a DNA-free nuclear receptor DNA binding domain sheds light on DNA-driven allostery in the glucocorticoid receptor. Scientific Reports 2018, 8(1), 13497. 
  • Okafor, C.D.; Pathak, M.F.; Fagan, C.E.; Bauer, N.C.; Cole, M.F.; Gaucher, E.A.; and Ortlund, E.A. Structural Analyses of Ancient, Modern and Consensus Elongation Factor TU proteins Reveal Strategies for Engineering Thermostability. Structure 2018, 26(1), 118-129. 
  • Mays, S.G.; Okafor, C.D.; Tuntland, M.L.; Whitby, R.J.; Dharmajan, V.; Stec, J.; Griffin, P.R.; Ortlund, E.A. Structure and Dynamics of the Liver Receptor Homolog 1-PGC1a Complex. Mol Pharmacol. 2017, 92(1), 1-11. 
  • Weikum, E.R.; Okafor, C.D.; D’Agostino, E.H.; Colucci, J.C.; and Ortlund, E.A. Structural Analysis of the Glucocorticoid Receptor Ligand-Binding Domain in Complex with Triamcinolone Acetonide and a Fragment of the Atypical Coregulator, Small Heterodimer Partner. Mol. Pharmacol. 2017, 92(1), 12-21. 
  • Okafor, C.D.; Lanier, K.A.; Petrov, A.S.; Athavale, S.S.; Bowman, J.C.; Hud, N.V.; and Williams, L.D. Iron Mediates Catalysis of Nucleic Acid Processing Enzymes: Support for Fe(II) as a Cofactor before the Great Oxidation Event. Nucleic Acids Res. 2017, 45, 3634-3642 
  • Mays, S.G.; Okafor, C.D.; Whitby, R.J.; Goswami, D.; Stec, J.; Flynn, A.; Dugan, M.; Griffin, P.R.; Jui, N.; Ortlund, E.A. Crystal Structures of the Nuclear Receptor, Liver Receptor Homolog 1, Bound to Synthetic Agonists Reveal a Novel Mechanism of Receptor Activation. J. Biol Chem, 2016, 291(49). 25281-25291