): This application seeks partial support for a 2 1/2 day meeting on """"""""Frontiers in Structural Biology of Membrane Proteins"""""""" to be held on November 9-12, 2000 at the Hilton Conference Center in Galveston, TX. At least one third of all genes in the human genome encode membrane proteins with at least one membrane-spanning helix. These proteins perform a vast repertoire of functions essential for life, and include pumps, solute transporters, channels, receptors, energy converters, and signal transducers. Mutations in membrane proteins have been associated with many diseases, and they are regarded as major targets for drug development. As a case in point, approximately 60 percent of the drugs in the current pharmacopoeia have G protein-coupled receptors, a superfamily of membrane proteins, as their target sites. Clearly, elucidating the mechanisms of action of membrane proteins requires both their functional characterization and knowledge of their three-dimensional structure at or close to atomic resolution. Yet, while more than 4000 structures of soluble proteins have been solved to resolutions better than 2.5 A, and more than one a day is being added to the protein data bank, the pace for solving the structure of membrane proteins is very slow with fewer than 20 high resolution structures known to date. The major difficulty for solving the structure of membrane proteins by X-ray crystallography is the generation of well-diffracting crystals. Recent advances in the crystallization of membrane proteins, as well as a new generation of synchrotron facilities, promise to greatly accelerate research in solving the structures of membrane proteins. Furthermore, NMR and electron crystallography are also promising tools. This symposium will offer a forum to discuss new approaches for solving membrane protein structures and developing structure-based drug design strategies. There will be approximately 100 attendees; the participants will include leaders in the structural biology of membrane proteins from Europe, Japan and the U.S., and a major objective is to recruit a new generation of scientists into this emerging field.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Conference (R13)
Project #
1R13GM062949-01
Application #
6319399
Study Section
Biophysical Chemistry Study Section (BBCB)
Program Officer
Chin, Jean
Project Start
2000-12-06
Project End
2001-12-05
Budget Start
2000-12-06
Budget End
2001-12-05
Support Year
1
Fiscal Year
2001
Total Cost
$5,000
Indirect Cost
Name
University of Texas Medical Br Galveston
Department
Neurosciences
Type
Schools of Medicine
DUNS #
800771149
City
Galveston
State
TX
Country
United States
Zip Code
77555