Ion channels and transporter protein play important roles in generating electrical signals and in communication between neurons mediated by chemical neurotransmitters. Action potentials, which causes neurotransmitters to be released into the synaptic cleft then to bind and activate receptors on the postsynaptic membrane and eventually leads to changes in the postsynaptic membrane potential, can be generated by the regulation of ion channel activity in response to different stimuli such as temperature, pressure, pH, oxygen, light, and some other signaling molecules. My lab aims to discover the molecular structures of those ion channels and neurotransmitter transporters related to neural electrical signal conduction in various physiological status including substrate binding, ion transporting, gating and activity regulating by other small molecules, and further reveal their working mechanisms with structural biology, electrophysiology and biochemistry ways.
Email:
Research Direction:1. Molecular mechanisms of neural signal transduction； 2.AAV-host recognition
Email:
Research Direction:Molecular mechanisms of neural signal transduction
Email:
Research Direction:Molecular mechanisms of neural signal transduction
Email:
Research Direction: Neurotransmitter transmission
Li, B.#, Hoel, C. M.#, & Brohawn, S. G.* (2021). Structures of Tweety Homolog Proteins TTYH2 and TTYH3 reveal a Ca2+-dependent switch from intra- to inter-membrane dimerization. Nature Communications.
Rietmeijer, R. A.#, Sorum, B.#, Li, B., & Brohawn, S. G.* (2021). Physical basis for distinct basal and mechanically gated activity of the human K+ channel TRAAK. Neuron.
Li, B.#, Rietmeijer, R. A.#, & Brohawn, S. G.* (2020). Structural basis for pH gating of the two-pore domain K+ channel TASK2. Nature.
Hu, C. W.#, Worth, M.#, Fan, D.#, Li, B.#, Li, H.#, Lu, L., Zhong, X., Lin, Z., Wei, L., Ge, Y., Li, L., & Jiang, J.* (2017). Electrophilic probes for deciphering substrate recognition by o-glcnac transferase. Nature Chemical Biology.
Li, B.#, Li, H.#, Hu, C. W., & Jiang, J.* (2017). Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase. Nature Communications.
Li, B., Li, H., Lu, L., & Jiang, J.* (2017). Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode. Nature Structural and Molecular Biology.
Li, B.#, Wang, Q.#, Pan, X., De Castro, I. F., Sun, Y., Guo, Y., Tao, X., Risco, C., Sui, S. F., & Lou, Z.* (2013). Bunyamwera virus possesses a distinct nucleocapsid protein to facilitate genome encapsidation. Proceedings of the National Academy of Sciences of the United States of America.
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