The Ontario Genomics Institute (OGI), together with the Structural Genomics Consortium (SGC) would like to announce an exciting opportunity that may enhance your research and expedite Ontario-based biomedical research and efforts in drug discovery.
The SGC has solved almost 1000 3-D protein structures of pharmaceutical or biomedical relevance. In the remaining two years of Phase II of the SGC, the major focus will continue to be human proteins involved in diseases or proteins of parasites that cause diseases such as malaria. Significant funding from the Ontario Ministry of Research and Innovation is providing an opportunity for the Ontario research community to nominate 200 human and parasitic proteins as targets that lack a publicly available structure. Purification protocols and expression clones will be made available to the research community for structures solved by the SGC and in a limited number of cases, this information will be available prior to the structure being determined.
This is a unique chance to engage renowned researchers in a world-class facility to solve the structures of proteins relevant to your research interests. The SGC hopes that by immediately releasing solved structures into the public domain and making available all reagents and methods, it will facilitate the research efforts of your group.
Interested? To nominate individual or sets of related protein targets do the following:
Fill out: Ontario Target Nomination Form
E-mail to: KFiebig@OntarioGenomics.ca
Deadline: Friday, January 29, 2010
Nominations will be forwarded to the SGC Scientific Committee, which will finalize a list of approved targets in March 2010. After this date, nominations will be accepted and reviewed on a quarterly basis.
The SGC will notify you regarding the status of your nominations and possibilities for collaboration. If one or more of your targets are selected, the SGC will contact you for any important information regarding expressing and purifying your protein target(s). Ultimately, the SGC will inform you when the structure of each protein is solved. If you made a successful nomination in previous years, your target is currently being pursued.
Several successful collaborations between SGC and Ontario researchers have resulted in the following publications:
Poondra RR, Kumar NN, Bijian K, Prakesch M, Campagna-Slater V, Reayi A, Reddy PT, Choudhry A, Barnes ML, Leek DM, Daroszewska M, Lougheed C, Xu B, Schapira M, Alaoui-Jamali MA, Arya P. 2009. Discovery of Indoline-Based, Natural-Product-like Compounds as Probes of Focal Adhesion Kinase Signaling Pathways. J Comb Chem. Jan 15. [Epub ahead of print]
Pardee KI, Xu X, Reinking J, Schuetz A, Dong A, Liu S, Zhang R, Tiefenbach J, Lajoie G, Plotnikov AN, Botchkarev A, Krause HM, Edwards A. 2009. The structural basis of gas-responsive transcription by the human nuclear hormone receptor REV-ERBbeta. PLoS Biol. 7(2):e43
Ravulapalli R, Campbell RL, Gauthier SY, Dhe-Paganon S, Davies PL. 2009.Distinguishing between calpain heterodimerization and homodimerization. FEBS J. 276(4):973-82.
Filippakopoulos P, Kofler M, Hantschel O, Gish GD, Grebien F, Salah E, Neudecker P, Kay LE, Turk BE, Superti-Furga G, Pawson T, Knapp S. 2008. Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation. Cell. 134(5):793-803.
Strushkevich N, Usanov SA, Plotnikov AN, Jones G, Park HW. 2008. Structural analysis of CYP2R1 in complex with vitamin D3. J Mol Biol. 380(1):95-106.
Bello AM, Poduch E, Fujihashi M, Amani M, Li Y, Crandall I, Hui R, Lee PI, Kain KC, Pai EF, Kotra LP. 2007. A potent, covalent inhibitor of orotidine 5'-monophosphate decarboxylase with antimalarial activity. J Med Chem. 50(5):915-21.
