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Articles by Baobin Li
Structural basis of phosphate export by human XPR1 - Nature Communications
Abstract Phosphorus in crucial for all living organisms. In vertebrate, cellular phosphate homeostasis is partly controlled by XPR1, a poorly characterized inositol pyrophosphate-dependent phosphate exporter. Here, we report the cryo-EM structure of human XPR1, which forms a loose dimer with 10 transmembrane helices (TM) in each protomer. The structure consists of a scaffold domain (TM1, TM3-4) and a core domain (TM2, TM5-10) structurally related to ion-translocating rhodopsins.
Structure basis for sugar specificity of gustatory receptors in insects - Cell Discovery
Dear Editor, Taste perception is essential for food selection and animal feeding behaviors1. While mammals use G protein-coupled receptors (GPCRs) for sweet and bitter tastant perception, insects such as fruit flies use a unique family of proteins called gustatory receptors (Grs)2. Attractive sweet compounds and aversive bitter compounds are perceived by different subsets of Grs distributed in distinct subpopulations of sensory cells, which eventually drive innate attraction or repellency1.
Coupling sensor to enzyme in the voltage sensing phosphatase - Nature Communications
Abstract Voltage-sensing phosphatases (VSPs) dephosphorylate phosphoinositide (PIP) signaling lipids in response to membrane depolarization. VSPs possess an S4-containing voltage sensor domain (VSD), resembling that of voltage-gated cation channels, and a lipid phosphatase domain (PD). The mechanism by which voltage turns on enzyme activity is unclear. Structural analysis and modeling suggest several sites of VSD-PD interaction that could couple voltage sensing to catalysis.
Semi-Supervised FMCW Radar Hand Gesture Recognition via Pseudo-Label Consistency Learning
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Physical basis for distinct basal and mechanically gated activity of the human K+ channel TRAAK
Highlights • The K2P TRAAK has physically distinct leak and mechanically activated open states • FHEIG syndrome-causing mutations promote mechanically activated openings • A pan-K2P activating mutation in the channel cavity promotes leak openings • Leak openings occur with TM4 down and mechanically activated openings with TM4 up Summary TRAAK is a mechanosensitive two-pore domain K+ (K2P) channel localized to nodes of Ranvier in myelinated neurons.
Structural basis for pH gating of the two-pore domain K+ channel TASK2
Abstract TASK2 (also known as KCNK5) channels generate pH-gated leak-type K+ currents to control cellular electrical excitability1,2,3. TASK2 is involved in the regulation of breathing by chemosensory neurons of the retrotrapezoid nucleus in the brainstem4,5,6 and pH homeostasis by kidney proximal tubule cells7,8. These roles depend on channel activation by intracellular and extracellular alkalization3,8,9, but the mechanistic basis for TASK2 gating by pH is unknown.
Erratum: PKM2 methylation by CARM1 activates aerobic glycolysis to promote tumorigenesis
In the version of this Article originally published, an amino acid (aa) range in Fig. 2a incorrectly read 390–53 aa. The correct range is 390–531 aa. In addition, two labels from Fig. 8j were displaced during production and instead appeared over Fig. 8g. These errors have now been corrected in the online version of the Article.
Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase
Exploiting our previously reported construct of OGA (residues 60–704 with the unstructured insert residues 401–552 replaced by a glycine–serine (GS) linker)20, we solved the structures of a mutant OGA -D175N (catalytically impaired but retaining the ability to bind substrate) in apo form and in complex with each of four synthetic glycopeptides.
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