Professor Shangyu Dang completed his undergraduate studies at Tsinghua University, where he worked in the lab of Professor Nieng Yan. During this time, he utilized X-ray crystallography to unravel the working mechanism of a fucose transporter (FucP). Following his Bachelor of Science degree, he pursued his Ph.D. in the lab of Professor Yigong Shi, also at Tsinghua University. His research focused on the structure and function of the presenilin homologue (PSH), which provided valuable insights into gamma-secretase and Alzheimer’s disease. After earning his Ph.D. from Tsinghua University in 2014, Prof. Dang joined the University of California San Francisco (UCSF) as a postdoctoral researcher. He worked in the lab of Professor Yifan Cheng, supported by a Human Frontier Science Program (HFSP) Long-term fellowship. During his postdoc training, he received comprehensive training in cryo-electron microscopy (cryo-EM) and successfully determined the structures of several membrane proteins, including TMEM16 and TRP family proteins, using the single-particle cryo-EM technique. Currently, Professor Shangyu Dang holds the position of Assistant Professor in the Division of Life Science at the Hong Kong University of Science and Technology (HKUST).

Research Interest

Our laboratory is dedicated to investigating the molecular mechanisms of biological macromolecules, with a specific focus on membrane proteins and protein-DNA complexes. We employ a multidisciplinary approach that encompasses various techniques such as X-ray crystallography, cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET), biochemistry, and electrophysiology.

In addition to our studies on fundamental biological processes, we are actively involved in the development of new methods in the fields of single-particle cryo-EM and cryo-ET. By tackling recurring challenges and expanding the applications of these techniques, we aim to contribute to their continuous improvement and advancement.

Ultimately, our research endeavors are driven by the goal of providing valuable information that can be utilized for structure-based drug design and development. We aim to shed light on the structural and functional aspects of proteins involved in human diseases, particularly those resulting from the dysfunction of these proteins. By gaining a deeper understanding of their molecular mechanisms, we hope to pave the way for the development of effective treatments in the near future.

Representative Publications

(*co-first author, ^#corresponding author, authors from the Dang Lab) >

1. Qin, Y.*, Yu, D.*, Wu, D.*, Dong, J.*, Li, W.T., Ye, C., Cheung, K.C., Zhang, Y., Wang, Y.^#, Shi, Y.S.^#, Dang, S.^#. Cryo-EM structure of TMEM63C suggests it functions as a monomer. Nature Communications 14, 7265 (2023).
2. Cai, L.*, Liu, H.*, Zhang, W., Xiao, S., Zeng, Q.^#, Dang, S.^#. Cryo-EM structure of cyanophage P-SCSP1u offers insights into DNA gating and evolution of T7-like viruses. Nature Communications 14, 6438 (2023).
3. Xu, Z.*, Feng, J.*, Yu, D.*, Huo, Y.*, Ma, X.*, Lam, W.H., Liu, Z., Li, X.D., Ishibashi, T., Dang, S.^#, Zhai, Y.^#. Synergism between CMG helicase and leading strand DNA polymerase at replication fork. Nature Communications 14, 5849 (2023).
4. Lin, J.*, Wu Y.*, Tian, G.*, Yu, D.*, Yang, E., Lan, W. H., Liu, Z., Jing, Y., Dang, S., Bao, X.^#, Wong, J. W. H.^#, Zhai, Y.^#, Li, X. D.^#. Menin “reads” H3K79me2 mark in a nucleosomal context. Science 379, 717-723 (2023).
5. Li, J.*, Dong, J.*, Wang, W.*, Yu, D.*, Fan, X., Hui, Y.C., Lee, C.S.K., Lam, W.H., Alary, N., Yang, Y., Zhang, Y., Zhao, Q., Chen, C.-L.^#, Tye, B.-K.^#, Dang, S.^#, Zhai, Y.^#. The human pre-replication complex is an open complex. Cell 186, 98-111 (2023).
6. Luo, M.*, Zhou, B.*, Reddemc, E.R.*, Tang, B.*, Chen, B.*, Zhou, R.*, Liu, H., Liu, L., Katsamba, P.S., Aua, K.-K., Man, H.-O., To, K.K.-W., Yuen, K.-Y., Shapiroc, L.^#, Dang, S.^#, Ho, D.D.^# and Chen, Z.^#, Structural insights into broadly neutralizing antibodies elicited by hybrid immunity against SARS-CoV-2. Emerging Microbes & Infections 12:1 (2023).
7. Xu, Y., Dang, S.. Recent Technical Advances in Sample Preparation for Single-Particle Cryo-EM. Front. Mol. Biosci. 9:892459 (2022).
8. Zhou, B.*, Zhou, R.*, Tang, B.*, Chan, J. F.-W.*, Luo, M.*, Peng, Q.*, Yuan, S.*, Liu, H.*, Mok, B.W.-Y., Chen, B., Wang, P., Poon, V.K.-M., Chu, H., Chan, C.C.-S, Tsang, J.Q.-L., Chan, C.C.-Y., Au, K.-K., Man, H.-O., Lu, L., To, K.K-W., Chen, H., Yuen, K.-Y., Dang, S.^#, Chen, Z.^#. A broadly neutralizing antibody protects Syrian hamsters against SARS-CoV-2 Omicron challenge. Nature Communications 13, 3589 (2022).
9. Cheng, J.*, Li, N.*, Huo Y., Dang, S., Tye, B.-K.^#, Gao, N.^#, Zhai, Y.^#. Structural insight into the MCM double hexamer activation by Dbf4-Cdc7 kinase. Nature Communications 13, 1396 (2022).
10. Fine, M.^#, Li, X.^#, Dang, S.^#. Structural insights into group II TRP channels. Cell Calcium 86, (2020).