Aik Lab
Chemical and Structural Biology Lab
Our Vision
3D structures of protein/nucleic acid complexes
We are interested in studying protein-nucleic acid complexes in various contexts, such as RNA metabolism, viral replication, and cancer. We also aspire to be innovative in designing therapies using structures of protein/nucleic acid complexes as guides.
Our Techniques
Structural Biology
Our core technique is macromolecular X-ray crystallography. We are also interested in using other structural biology tools such as cryo-electron microscopy and NMR to obtain structural information of macromolecules.
Chemical Biology
We also take advantage of powerful techniques in chemistry to detect, analyse and probe biomolecules. Examples of techniques we frequently use are mass spectrometry and liquid chromatography. We also incorporate molecular biology techniques in our research.
Our Research Highlights
Structures of ALKBH5-m6A RNA complexes
March 25, 2022
We determined structures of ALKBH5, an m6A demethylase, in complex with a substrate RNA containing m6A modification. The structures gave unprecedented insights into how ALKBH5 recognises the Gm6AC consensus motif and its mechanisms of m6A demethylation involving a proton shuttle network in the active site. Congratulations to Simran and Samson as main contributors to our publication in Nucleic Acids Research!
https://doi.org/10.1093/nar/gkac195
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Structure-based design of potent and selective FTO Inhibitors
November 11, 2021
We recently published our work on structure-based design FTO inhibitors, in collaboration with the Schofield Group from the University of Oxford. The fat mass and obesity associated protein, FTO, is an RNA m6A oxygenase involved in cancer and obesity; therefore FTO is a potential therapeutic target. Congratulations to Samson and Yi Min who contributed to this article in the Journal of Medicinal Chemistry!
https://pubs.acs.org/doi/abs/10.1021/acs.jmedchem.1c01204
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Structural basis for Rab23 activation and a loss-of-function mutation in Carpenter syndrome
January 16, 2025
We determined high-resolution crystal structures of human Rab23 and the human Rab23 Y79del clinical mutant, in complex with GDP and GMPPNP, a nonhydrolysable GTP analog, respectively. Supported by in vitro biochemical and functional analyses, we demonstrated that the Y79 deletion mutant exhibited structural distortions in the switch II region relative to that of the WT. The structural changes potentially disrupted the binding of Rab23 Y79del to its interacting partners, thus leading to a loss-of-function and the development of Carpenter syndrome.Congratulations to Yat Yin and Hanbin who contributed to this article in the Journal of Biological Chemistry!
Get in Touch
Department of Chemistry
Hong Kong Baptist University
Kowloon Tong, Hong Kong SAR
HKBU site: https://chem.hkbu.edu.hk/aik
+852 3411 6682
