By John Vetterli [CC-BY-SA-2.0 (http://creativecommons.org/licenses/by-sa/2.0)], via Wikimedia Commons

The SGC Toronto scientists seek to determine the 3D structures of human proteins of therapeutic relevance to diseases such as cancer and metabolic disorders. We have a particular focus on proteins involved in intracellular small molecule metabolism, enzymes involved in the transfer of methyl, acetyl and Ubiquitin-like groups, proteases and nucleotide triphosphatases. We are also investigating proteins from Plasmodium falciparum (and its apicomplexan relatives) which causes malaria.

The SGC Toronto laboratories, under the direction of Prof. Cheryl Arrowsmith, are housed within the Faculty of Medicine at the University of Toronto and located in the MaRS Discovery District, at the heart of cosmopolitan Toronto. Scientists at SGC Toronto are affiliated with several University Departments including the Banting and Best Department of Medical Research, the Departments of Physiology, Pharmacology, Medical Biophysics, and Medical Genetics and Microbiology.

The SGC Toronto laboratories have research efforts in biotechnology, laboratory automation, protein expression, protein crystallization and X-ray crystallography.

The SGC encourages collaborations with laboratories from across the globe on proteins that are currently on our target list. In addition, scientists from Ontario can nominate protein targets of pharmaceutical or biomedical relevance via the Ontario Genomics Institute. Nominated targets should be human proteins or proteins from human parasites for which a 3D protein structure will aid biomedical research. Download target nomination form here.


Watch this brief video highlighting the SGC and its innovative work at the University of Toronto.

There are currently no open vacancies with the SGC Toronto. Please check back periodically for opportunities which may arise in any of our sites.

 

Discovery of a Potent and Selective Coactivator Associated Arginine Methyltransferase 1 (CARM1) Inhibitor by Virtual Screening.
Ferreira de Freitas R, Eram MS, Smil D, Szewczyk MM, Kennedy S, Brown PJ, Santhakumar V, Barsyte-Lovejoy D, Arrowsmith CH, Vedadi M, Schapira M
J. Med. Chem.. 08.07.2016 . doi: 10.1021/acs.jmedchem.6b00668
PMID: 27390919

Methyltransferase inhibitors for modulation of the epigenome and beyond.
Schapira M, Arrowsmith CH
Curr Opin Chem Biol. 16.06.2016 33:81-87. doi: 10.1016/j.cbpa.2016.05.030
PMID: 27318562

Structure and function of histone methylation-binding proteins in plants.
Liu Y, Min J
Biochem. J.. 15.06.2016 473(12):1663-80. doi: 10.1042/BCJ20160123
PMID: 27288029

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