Proteins are involved in virtually every process within biological systems, and the function that a protein assumes depends on its structure. Determining the structure of a protein is of fundamental importance to understanding protein interactions, the role of proteins in diseases and disorders, drug design and more. Cryo-electron microscopy (cryo-EM) was developed as a cutting-edge alternative to X-ray crystallography, and alleviates the need for crystallization. With recent advances in electron detection and image processing, the resolution by cryo-EM is now beginning to rival X-ray crystallography. Our goal is to employ cryo-EM to determine high resolution structures of important membrane protein complexes involved in cellular signaling, including cellular receptors and ion channels. We also combine structural approaches with functional studies to reveal the structure-function relationships of these membrane proteins.

Structure Gallery
C-MET/HGF 2:2 asymmetric complexes in the active state. This study reveals that one HGF molecule is sufficient to induce a specific dimerization mode of c-MET by utilizing two distinct interfaces
September 21, 2018/by Academic Web PagesScap alone or with Insig bound. This study reveals a large rotation of the luminal L1-L7 domain upon the binding of Scap to Insig.
September 22, 2018/by Academic Web PagesSema3A/PlexinA4/Neuropilin tripartite complex
September 23, 2018/by Academic Web PagesSTRIPAK complex: a large, multisubunit protein phosphatase 2A assembly that is critical in regulating the Hippo pathway
September 24, 2018/by Academic Web PagesMap
Bai Lab
UT Southwestern Medical Center
5323 Harry Lines Boulevard
Dallas, TX 75390
Xiaochen.Bai@utsouthwestern.edu