By John Vetterli [CC-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.

A bioinformatics Postdoctoral Fellow position is available immediately to work in close collaboration within SGC and OCI/PMCC in Toronto. We offer an interdisciplinary research environment with exciting challenges on novel biological data and leading-edge expertise in one of today's most dynamic scientific disciplines. We are looking for people that are highly qualified and motivated to join our interdisciplinary team.

Closing Date:
Monday 30th November 2015
Design of a fluorescent ligand targeting the S-adenosylmethionine binding site of the histone methyltransferase MLL1.
Luan Y, Blazer LL, Hu H, Hajian T, Zhang J, Wu H, Houliston S, Arrowsmith CH, Vedadi M, Zheng YG
Org. Biomol. Chem.. 06.11.2015 . doi: 10.1039/c5ob01794g
PMID: 26541578

Structural basis for substrate recognition by the human N-terminal methyltransferase 1.
Dong C, Mao Y, Tempel W, Qin S, Li L, Loppnau P, Huang R, Min J
Genes Dev.. 05.11.2015 . doi: 10.1101/gad.270611.115
PMID: 26543161

Structural basis for the regulatory role of the PPxY motifs in the thioredoxin-interacting protein TXNIP.
Liu Y, Lau J, Li W, Tempel W, Li L, Dong A, Narula A, Qin S, Min J
Biochem. J.. 02.11.2015 . doi: 10.1042/BJ20150830
PMID: 26527736

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