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.

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


Structural biology: HDAC6 finally crystal clear.
Liu Y, Li L, Min J
Nat. Chem. Biol.. 18.08.2016 12(9):660-1. doi: 10.1038/nchembio.2158
PMID: 27538024

Structural basis of arginine asymmetrical dimethylation by PRMT6.
Wu H, Zheng W, Eram MS, Vhuiyan M, Dong A, Zeng H, He H, Brown P, Frankel A, Vedadi M, Luo M, Min J
Biochem. J.. 01.08.2016 . doi: 10.1042/BCJ20160537
PMID: 27480107

Structure-Activity Relationship Studies for Enhancer of Zeste Homologue 2 (EZH2) and Enhancer of Zeste Homologue 1 (EZH1) Inhibitors.
Yang X, Li F, Konze KD, Meslamani J, Ma A, Brown PJ, Zhou MM, Arrowsmith CH, Kaniskan HÜ, Vedadi M, Jin J
J. Med. Chem.. 28.07.2016 . doi: 10.1021/acs.jmedchem.6b00855
PMID: 27468126

glqxz9283 sfy39587stf02 mnesdcuix8