Zongchao Jia, Queen’s University

Profile photo of Zongchao Jia, expert at Queen’s University

Department of Biomedical and Molecular Sciences Professor Kingston, Ontario jia@queensu.ca Office: (613) 533-6277

Bio/Research

Protein crystallography is a powerful tool capable of revealing atomic details of protein. The technique has been widely used to determine 3-D structures of proteins, multi-domain large protein complexes, protein-DNA interactions etc. Protein crystallography has in the last decade advanced greatl...

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Bio/Research

Protein crystallography is a powerful tool capable of revealing atomic details of protein. The technique has been widely used to determine 3-D structures of proteins, multi-domain large protein complexes, protein-DNA interactions etc. Protein crystallography has in the last decade advanced greatly and made a major contribution to the fundamental understanding of biological processes and provided insights into problems of molecular recognition and biological control of importance to medicine and the pharmaceutical industry. Our research, currently focusing on structure-function studies of a number of biologically significant proteins, is largely funded by Canadian Institutes of Health Research (CIHR) and Natural Sciences and Engineering Research Council of Canada (NSERC). It includes cancer structural biology, structural genomics, phosphatase kinase and EF-hand calcium-binding proteins. Please visit our website to find out more.

Phosphatases/kinases are involved in a wide range of cellular processes. We are working on a number of novel bacterial kinases and phosphatase. Along with structural characterization, we are also interested in probing their cellular and biochemical function by using a wide variety of approaches including cell biology, biochemical and biophysical methods.

Bacterial structure genomics provides us with an opportunity to systematically study a selected group of protein. We are particularly interested in proteins with "unknown" function and protein-protein complex structures. Based on the structural insights, we hope to obtain important clues for the function, and subsequently verify it by biochemical experiments.

EF-hand proteins such as calmodulin bind to calcium ions to elicit their biological function. We are interested in studying calcineurin, a prominent protein phosphatase, and its activation by calmodulin and calpain, a calcium-dependent protease.

We are working on a group of cancer-associated protein targets. While there is strong clinical/genetic evidence substantiating the notion that these proteins are clearly involved in cancer, unfortunately the biochemical function of most of these proteins, if not all, are not known at all. In this work, we will determine the 3-D structures of these targets, based on which biochemical and biophysical characterization will be carried out to gain insights into their biological function.


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