Duanfang Cao, Ph.D, Associate Professor Members of the Youth Innovation Promotion Association, CAS  National Laboratory of Biomacromolecules, IBP Structural and functional studies of macromolecules, virus structure and virus entry E-mail: caodf@ibp.ac.cn Tel: 010-64887082 Zip code: 100101 Chinese personal homepage

Biography & Introductions

2005/09-2009/06 Wuhan University of Science and Technology, Bachelor of Medicine

2009/09-2015/12 University of Chinese Academy of Sciences, Ph.D

2016/01-2018/12 Institute of Biophysics, CAS Assistant Professor 

2019/12-present  Institute of Biophysics, CAS Associate Professor 

Research interest  

(1) Glycoproteins of enveloped virus determine virus entry into host cells and host tropism, which is an important target for therapeutics development. Investigating the structure information of virus glycoprotein in different fusion states, should help to understand the virus entry mechanism and develop effective vaccine and drugs. We solved the cryo-EM structure of the MERS-CoV and SARS-CoV Spike protein in its pre-fusion trimeric conformation. The structures present two conformations of the S1 subunit with the receptor binding region buried or exposed, demonstrating an inherently flexible RBD that is readily recognized by the receptor. This work provides an important framework to understand the entry mechanism of coronavirus, and suggest ways for preventing or controlling future outbreaks of MERS-CoV and SARS-CoV. It will be of particular interest for us to further investigate the glycoprotein structures and virus entry mechanism of enveloped virus.

(2) SIRT1 is the human homolog of yeast Sir2, which is the founding member of the sirtuins family of NAD+ dependent deacetylases. SIRT1 is involved in the regulation of various biological pathways, such as chromatin remodeling, gene regulation, metabolism, tumor biogenesis and aging. We solved the crystal structure of SIRT1 holoenzyme in complex with the p53-AMC peptide and three activator resveratrol molecules, revealed the binding details of substrate peptide, and the molecular mechanism of resveratrol stimulation. The extend NTD of SIRT1 is responsible for the allosteric activation of SIRT1 activity by resveratrol. This work provides valuable insights into regulation of SIRT1 activity and should benefit the development of new effective SIRT1 activating compounds

Selected Publications

I、Research articles

1. Yuan Yuan^#, Duanfang Cao^#, Yanfang Zhang^#, Jun Ma^#, Jianxun Qi, Qihui Wang, Guangwen Lu, Ying Wu, Jinghua Yan, Yi Shi*, Xinzheng Zhang*, and George F. Gao*. Cryo-Em Structures of Mers-Cov and Sars-Cov Spike Glycoproteins Reveal the Dynamic Receptor Binding Domains. Nature Communications. 8 (2017).

2. Duanfang Cao^#, Mingzhu Wang, Xiayang Qiu, Dongxiang Liu, Hualiang Jiang, Na Yang*, and Rui-Ming Xu*. Structural Basis for Allosteric, Substrate-Dependent Stimulation of Sirt1 Activity by Resveratrol. Genes & Development. 29 (2015), 1316-25.

II、Invited reviews

Duanfang Cao^#, Na Yang*. Structure and Catalytic Mechanisms of Histone Deacetylases. Progress in Biochemistry and Biophysics. 42 (2015), 978-93.

　　 

From Duanfang Cao, 2017-12-23 update