David R. Davies, Ph.D.


LMB
MOLECULAR STRUCTURE SECTION
NIDDK, National Institutes of Health
Building 5 , Room 338
5 Memorial Dr.
Bethesda, MD 20814
Tel: 301-496-1295

Email: david.davies@nih.gov

David R. Davies, Ph.D.

Education / Previous Training and Experience:
B.A., Oxford, 1949
Ph.D., Oxford, 1952


Research Statement:

Structure Analysis of Proteins and Nucleic Acids

We have a broad range of interests in structures of biological macromolecules. These include enzyme complexes, protein/nucleic acid complexes, prion proteins. Current research includes:

  1. An investigation into the crystal structure and mechanism of action of the Toll-like receptors of the innate immune system.

  2. Several other proteins under investigation. They include an anti-anthrax lyase.


Selected Publications:

1. Chiu TK, Kubelka J, Herbst-Irmer R, Eaton WA, Hofrichter J, Davies DR  High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.  Proc Natl Acad Sci U S A (102): 7517-22, 2005. [Full Text/Abstract]

2. Bell JK, Botos I, Hall PR, Askins J, Shiloach J, Segal DM, Davies DR  The molecular structure of the Toll-like receptor 3 ligand-binding domain.  Proc Natl Acad Sci U S A (102): 10976-80, 2005. [Full Text/Abstract]

3. Umland TC, Wolff EC, Park MH, Davies DR  A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex.  J Biol Chem (279): 28697-705, 2004. [Full Text/Abstract]

4. Bell JK, Mullen GE, Leifer CA, Mazzoni A, Davies DR, Segal DM  Leucine-rich repeats and pathogen recognition in Toll-like receptors.  Trends Immunol (24): 528-33, 2003. [Full Text/Abstract]

5. Umland TC Taylor KL Rhee S Wickner RB Davies DR  The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p.  Proc Natl Acad Sci U S A (98): 1459-64, 2001. [Full Text/Abstract]




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Page last updated: December 15, 2008

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