The Protein Expression Laboratory (PEL) studies the structure and function of viral proteins, primarily those of the human immunodeficiency virus (HIV-1) and the hepatitis B virus (HBV). The PEL also studies the interactions of these viral proteins with host proteins.
Most structural biology techniques, especially those for studying the three-dimensional structures of proteins, require large quantities of highly purified, monodisperse, and correctly folded proteins. The PEL uses recombinant DNA techniques to produce proteins both for in-house use and for collaborating scientists. It employs techniques such as analytical ultracentrifugation, UV-CD, NMR, X-ray crystallography, and cryo-electron microscopy to characterize and determine the structures of these proteins and their complexes.
Paul T. Wingfield, Ph.D. received his doctoral degree from Dundee University, Scotland, in 1975 following his work on the composition and structure of components of the inner membrane of beef heart mitochondria under the supervision of Prof. Peter B. Garland. From 1975 to 1977 he did postdoctoral training with Profs. Alex N. Glazer & Robert J. Delange at the University of California, Los Angeles. Following a position as Staff Scientist in the Biological Structures Division at the European Molecular Biology Laboratory, Heidelberg, Germany (1977 to 1981), Dr. Wingfield served as Department Head of Protein Chemistry, first at Biogen (1981 to 1987) and then at the Glaxo Institute for Molecular Biology (1987 to 1989) in Geneva, Switzerland, followed by a position as Manager of the Department of Molecular Genetics & Protein Chemistry at Pfizer Central Research, Groton, Connecticut (1991 to 1992). Since then, he has served as Laboratory Chief of the Protein Expression Laboratory (NIAMS), and as Acting Laboratory Chief of the Laboratory of Structural Biology Research (NIAMS).
- Stahl SJ, Watts NR, Rader C, DiMattia MA, Mage RG, Palmer I, Kaufman JD, Grimes JM, Stuart DI, Steven AC, Wingfield PT. Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev. J Mol Biol. 2010;397(3):697-708.
- DiMattia MA, Watts NR, Stahl SJ, Rader C, Wingfield PT, Stuart DI, Steven AC, Grimes JM. Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element. Proc Natl Acad Sci U S A. 2010;107(13):5810-4.
- Jedidi I, Zhang F, Qiu H, Stahl SJ, Palmer I, Kaufman JD, Nadaud PS, Mukherjee S, Wingfield PT, Jaroniec CP, Hinnebusch AG. Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX domain, to recruit mediator to target genes in vivo. J Biol Chem. 2010;285(4):2438-55.
- Dearborn AD, Eren E, Watts NR, Palmer IW, Kaufman JD, Steven AC, Wingfield PT. Structure of an RNA Aptamer that Can Inhibit HIV-1 by Blocking Rev-Cognate RNA (RRE) Binding and Rev-Rev Association. Structure. 2018.
- Lakomek NA, Kaufman JD, Stahl SJ, Wingfield PT. HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation. Structure. 2014;22(9):1311-1321.
Related Scientific Focus Areas
Molecular Biology and Biochemistry
Microbiology and Infectious Diseases
This page was last updated on Friday, December 11, 2020