Dr. Jian Yang
B.Sc. (Peking), Ph.D. (Saskatchewan)Associate Professor of Pharmacy
Dr. Yang joined the College in September 2003.
Undergraduate teaching in the areas of Medicinal Chemistry and Structural Biochemistry.
Dr. Yang’s research laboratory is interested in understanding the structural basis for important biological functions using protein crystallography as a tool. Currently, the laboratory is working on two major research projects.
1. The PCP biodegradation pathway: This pathway contains three enzymes, PCP hydroxylase, TCHQ dehalogenase and DCHQ dioxygenase. PCP hydroxylase catalyzes the conversion of PCP to TCHQ, which is the rate-limiting step in the pathway. TCHQ dehalogenase catalyzes the two successive steps of reduction reactions, converting TCHQ to TriCHQ and then to DCHQ. DCHQ is a common metabolic intermediate of PCP and several other chloroaromatic compounds. DCHQ dioxygenase is so far the only reported enzyme that degrades DCHQ. The end product of the ring cleavage of DCHQ is 2-chloromaleylacetate.
2. The Toll receptor signaling pathway: This pathway was first identified in Drosophila in the study of early embryonic development. Subsequent studies reveal that the Toll receptor signaling pathway is one of the major signaling pathways for Drosophila innate immunity. The Toll signaling pathway is activated by Gram-positive bacteria and fungi, whereas the immune deficiency (Imd)/Relish pathway is responsible for defense against Gram-negative pathogens. The Toll receptor itself does not recognize microbial patterns. Its activation requires a dimeric extracellular protein, Spätzle. The activation of the Toll receptor by Spätzle initiates the cytoplasmic-nuclear translocation of a family of transcription factors in the NF-KB family and produces the antimicrobial peptide drosomycin.
J. Yang, Y. Wang, E.M. Woolridge, G.A. Petsko, J.W. Kozarich, and D. Ringe, 2004. Crystal Structure of 3-Carboxy-cis,cis-Muconate Lactonizing Enzyme from Pseudomonas putida, a Fumarase Class II Type Cycloisomerase: Enzyme Evolution in Parallel Pathways, Biochemistry, 43, 10424-10434.
J. Yang, L. Liu, D. He, X. Song, X. Liang, J.Z. Zhao and G.W. Zhou, 2003. Crystal Structure of Human Protein Tyrosine Phosphatase SHP-1, Journal of Biological Chemistry, 278, 6516-6520.
J. Yang, T. Niu, A. Zhang, A.K. Mishra, J.Z. Zhao and G.W. Zhou, 2002. Relation Between the Flexibility of the WPD Loop and the Activity of the Catalytic Domain of Protein Tyrosine Phosphatase SHP-1, Journal of Cellular Biochemistry, 84, 47-55.
J. Yang, Z. Cheng, T. Niu, X. Liang, J.Z. Zhao, and G.W. Zhou, 2001. Protein Tyrosine Phosphatase SHP-1 Specifically Recognizes C-terminal Residues of its Substrates via Helix-alpha0, Journal of Cellular Biochemistry, 83, 14-20.
J. Yang, Z. Cheng, T. Niu, X. Liang, J.Z. Zhao and G.W. Zhou, 2000. Structural Basis for Substrate Specificity of Protein Tyrosine Phosphatase SHP-1. Journal of Biological Chemistry, 275, 4066-4071.
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