Research


Structural Biology and Epigenetics

Dr. Chengmin Qian

Dr Qian, Chengmin (錢程民)

Assistant Professor, Department of Biochemistry

BSc (Anhui Normal); PhD (Nanjing)

Contact
Email: cmqian@hku.hk
Tel: (852) 2819 2820
Office: L3-82, Laboratory Block, 21 Sassoon Road, Hong Kong

Postgraduate Research Projects Available:

  • Structure and Mechanism of Protein Module in Epigenetics
  • Structural Biology of DNA Damage & Repair

Postitons Available:

  • We currently have the opportunity to recruit a highly-motivated postdoctoral fellow to work on the structural mechanisms of intra-S-phase checkpoint activation in response to DNA damage. The candidate should have a background in protein crystallography or protein NMR.
  • A research assistant position is available in the lab. The candidate is required to have hands-on experience with protein cloning, expression and purification, a background in structural biology is preferred. The successful candidate will participate in our ongoing studies on structure & mechanism of novel tumor suppressors involved in damaged DNA repair.

    • Applicants should email their CV and a summary of research experience to Dr. Chengmin Qian (cmqian@hku.hk)

Research Description:

Epigenetic changes play essential roles in normal development and human diseases. Aberrant epigenetic alternations have been implicated in many human cancers and inherited syndromes. To understand how epigenetic modifications occur during normal development, adult cell renewal and disease will significantly help to prevent, diagnose and treat epigenetic-related diseases. A major challenge in the field of epigenetics is to define the connection between distinct epigenetic modification and specific biological function. My current research is directed at understanding molecular mechanisms of epigenetic modifications at atomic resolution by using protein NMR and X-ray crystallography. We are studying chromatin modifying enzymes that establish different epigenetic modifications, and readout proteins that interpret epigenetic modifications. Our ultimate goal is to apply structure-based rational design method to develop small chemical compounds capable of modulating these epigenetic processes under physiological conditions.



Publications, Achievements, and Grants:

Selected Publications:

  • Xie S, Jean J, Qian C (2012). UHRF1 Double Tudor Domain and the Adjacent PHD Finger Act Together to Recognize K9me3-containing Histone H3 Tail. Journal of Molecular Biology 415, 318-28.
  • Qian C, Li S, Jakoncic J, Zeng L, Walsh M, Zhou M (2008). Structure and hemimethylated CpG binding of the SRA domain from human UHRF1. Journal of Biological Chemistry 283, 34490-4.
  • Qian C, Zhou M (2006). SET domain protein lysine methyltransferase: structure, specificity and catalysis. Cellular and molecular life sciences 63, 2755-2763.
  • Qian C, Wang X, Manzur K, Sachchidanand, Zeng L, Farooq A, Zhou M (2006). Structural insights of specificity and catalysis of a dimeric viral SET domain, a histone H3 lysine-27 methyltransferase. Journal of Molecular Biology 359, 86-96.
  • Qian C, Zhang Q, Li S, Zeng L, Walsh M, Zhou M (2005). Structure and chromosomal binding of SWIRM domain. Nature Structural and Molecular Biology 12, 1078-1085.
  • Qian C, Zhang Q, Wang X, Zeng L, Farooq A, Zhou M (2005). Structure of the adaptor protein p14 reveals a profilin-like fold with distinct function. Journal of Molecular Biology, 347, 309-321.
  • Qian C, Zeng L, Farooq A, Zhou M (2004). Resonance assignments for the endosomal adaptor protein p14. Journal of Biomolecular NMR 30, 367-368.
  • Qian C, Yao Y, Tong Y, Wang J, Tang W (2003). Structural Analysis of Zinc-substituted cytochrome c. Journal of Biological Inorganic Chemistry 8, 394-400.
  • Qian C, Yao Y, Ye K, Wang J, Tang W, Wang Y, Wang W, Lu J, Xie Y, Huang Z (2001). Effects of Charged Amino Acid Mutation on the Solution Structure of Cyotchrome b5 and Binding between Cyotchrome b5 and Cytochrome c. Protein Science 10, 2451-2459.
  • Qian C, Yao Y, Wu Y, Tang W (2000). Kinetic Studies of Imidazole and Its Methyl Derivative Binding to Metmyoglobin: Effects of Substitute Methyl on the Binding Affinity. Biometals 13, 267-272.
  • Ma D, Wu Y, Qian C, Tang W, Wang Y, Wang W, Lu J, Xie Y, Huang Z (1999). Effects of Some Charged Amino Acid Mutations on the Electron Self-exchange Kinetics of Cytochrome b5. Inorganic Chemistry 38, 5749-5754.