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Long Li



Emai: long_li(AT)pku.edu.cn




Research Interest

We are interested in the trans-membrane movements of the biological macromolecules. Cells and organelles are surrounded by the biological membranes that consist of lipid bilayers and membrane proteins. The membranes enclose and protect the cells while remaining open to communication, signaling, and other cellular processes. Therefore, the trans-membrane movements of biological macromolecules are critical for fundamental physiological activities. The movements are dynamic, yet ordered and precisely regulated. At the molecular level, the movements are driven by specific recognitions between proteins and lipids. A large number of membrane proteins function as translocases and translocation channels. We employ the biochemistry and structural biology approaches to study the membrane proteins involved in trans-membrane movements.  Our study will advance our knowledge on basic cell research, but also provide valuable insight into therapy for the human diseases related to malfunction of the trans-membrane movements. 


Selected publications

1. Li L*#, Park E*, Ling J, Ingram J, Ploegh H, Rapoport TA#. Nature. 2016 Mar 17;531(7594):395-9. Crystal structure of a substrate-engaged SecY protein-translocation channel. (* equal contribution; # co-corresponding authors)

2. Li L, Fierer JO, Rapoport TA, Howarth M. J Mol Biol. 2014 Jan 23;426(2):309-17. Structural analysis and optimization of the covalent association between SpyCatcher and a peptide Tag.

3. Li L, Jose J, Xiang Y, Kuhn RJ, Rossmann MG. Nature. 2010. Dec 2; 468(7324):705-8. Structural changes of envelope proteins during alphavirus fusion. (Cover image of the issue)

4. Li L, Lok SM, Yu IM, Zhang Y, Kuhn RJ, Chen J, Rossmann MG. Science. 2008 Mar 28; 319(5871):1830-4. The flavivirus precursor membrane-envelope protein complex: structure and maturation.


5. Yu IM, Zhang W, Holdaway HA, Li L, Kostyuchenko VA, Chipman PR, Kuhn RJ, Rossmann MG, Chen J. Science. 2008 Mar 28;319(5871):1834-7. Structure of the immature dengue virus at low pH primes proteolytic maturation.


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