|
Honors
Proposal Review Panel, SSRL, 2002-present
Member, American Crystallographic Association
Member, American Chemical Society
Member, American Association for the Advancement of Science
U.S. National Committee for Crystallography, 2002-2007
Newsletter Editor, American Crystallographic Association, 1994-2001
Research
The focus in my group is on the application of X-ray crystallographic techniques to determine the three-dimensional structures of biologically interesting macromolecules. Understanding the arrangements of atoms in molecules is useful for asking questions about their chemistry and function.
We are interested in a range of proteins and collaborate extensively with investigators whose emphasis is on the chemistry and biology of the molecules. Here’s a partial list of structure determinations currently underway in my lab.
Rhodopsin. This G protein-coupled receptor is the photo-active molecule in the visual system. In response to light, it initiates a signaling cascade that results in signals being sent to the brain. We have solved the ground-state structure as well as a photo-activated form of the protein. We are also pursuing studies of rhodopsin in complex with its protein ligands. This work is being done in collaboration with Kris Palczewski at Case-Western Reserve University.
Streptavidin. Biotin binds very strongly to streptavidin, and we want to understand the intermolecular interactions involved. In collaboration with Pat Stayton (Univ. of Washington) and Terry Lybrand (Vanderbilt Univ.), we are applying biophysical, computational and crystallographic methods to understand how the protein recognizes its small molecule ligands.
In addition to these two major projects, we are also collaborating with other Univ. of Washington faculty on molecular structures of importance for their functional studies. We currently have projects underway with Rachel Klevit (Biochemistry), Bill Parson (Biochemistry), Steve Libby (Laboratory Medicine), Steve Moseley (Microbiology), Evgeni Sokurenko (Microbiology), Bill Atkins (Medicinal Chemistry), and Rheem Totah (Medicinal Chemistry).
For additional information, please link to my personal Home
Page.
Selected
Publications
Korotkova, N., Y. Yang, I. Le Trong, E. Cota, B. Demeler, J. Marchant, W.E. Thomas, R.E. Stenkamp, S.L. Moseley and S. Matthews 2008 Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation. Molecular Microbiology, 67(2), 420-434.
Le Trong I. and R.E. Stenkamp 2007 An alternate description of two crystal structures of phospholipase A2 from Bungarus caeruleus. Acta Cryst. D63(4), 548-549.
Lodowski, D.T., D. Salom, I. Le Trong, D.C. Teller, J.A. Ballesteros, K. Palczewski and R.E. Stenkamp 2007 Crystal Packing Analysis of Rhodopsin Crystals. J. Struct. Biol., 158, 455-462.
Salom, D., D.T. Lodowski, R.E. Stenkamp, I. Le Trong, M. Golczak, B. Jastrzebska, T. Harris, J.A. Ballesteros and K. Palczewski 2006 Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc. Natl. Acad. Sci., USA, 103, 16123-16128.
Korotkova, N., I. Le Trong, R. Samudrala, K. Korotkov, C.P. Van Loy, A.-L. Bui, S. Moseley and R.E. Stenkamp 2006 Crystal structure and mutational analysis of the DaaE adhesin of Escherichia coli. J. Biol. Chem., 2006. 291(31), 22367-22377.
Le Trong, I., D.G.L. Aubert, N.R. Thomas and R.E. Stenkamp 2006 The high-resolution crystal structure of (+)-epi-biotin bound to streptavidin. Acta Crystallographica, D62, 576-581.
Hyre, D.E., I. Le Trong, E.A. Merritt, J.F. Eccleston, N.M. Green, R.E. Stenkamp and P.S. Stayton 2006 Cooperative hydrogen-bond interactions in the streptavidin-biotin system. Protein Science, 15, 459-467.
Le Trong, I., N. Humbert, T.R. Ward and R.E. Stenkamp 2006 Crystallographic analysis of a full-length streptavidin and its C-terminal polypeptide bound in the biotin binding site. J. Mol. Biol., 356, 738-745.
|
Box 357350 