Understanding protein structure-function relationships, he added, is central to understanding the machinery of lifehow protein complexes function in health and what goes wrong in disease.
The JCSGPast, Present, and Future
Wilson says that the JCSG's initial goal was to build a pipeline to explore the feasibility of applying high-throughput methods to structural biology and then see just how many structures could be could actually be solved in any given year.
"Our high-throughput structural genomic pipeline started modestly in the initial exploration phase of the PSI-1 (2000-2005), but has solved more than 200 novel structures a year for the past three years in a row in PSI-2 (2005-2010)an unthinkable feat at the onset of this projectand more than 1,150 structures to date," Wilson said. "The vast majority of these structures have been solved by X-ray crystallography, but NMR is now playing an important role in tacking certain classes of proteins due to Professor Kurt Wthrich and his team at Scripps Research joining the JCSG in the latter part of PSI-1."
Wilson adds that processing such large numbers of targets and enormous amounts of associated data has resulted in the development of new technologies and methodologies that facilitate high-throughput structural genomics and push the frontiers of structural biology. "These new technologies, when feasible, have been converted to free-access, web-based tools and applications that include XtalPred, Structure Validation, and Ligand Database servers, and the TOPSAN annotation portal," Wilson said. TOPSAN, The Open Protei
|Contact: Mika Ono|
Scripps Research Institute