55 Papers
81 Citations
Xiaochun Li is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Chemistry & Biology. The author has an hindex of 20, co-authored 37 publications. Previous affiliations of Xiaochun Li include Tsinghua University & Howard Hughes Medical Institute.
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Papers
Structures of human Patched and its complex with native palmitoylated sonic hedgehog.
TL;DR: High-resolution structures of the human plasma membrane protein patched 1 alone and in complex with the native form of the ligand sonic hedgehog are determined and atomic insights are provided into the recognition of the N-terminal domain of HH (HH-N) by PTCH1, which offers a structural basis for cooperative binding of HH-N to various receptors and serves as a molecular framework for HH signalling and its malfunction in disease.
176
Clues to the mechanism of cholesterol transfer from the structure of NPC1 middle lumenal domain bound to NPC2
TL;DR: The crystal structure of an NPC1–NPC2 complex is presented and it is shown that the amino acid residues that are important for this interaction in vitro are also important for cholesterol export from lysosomes of cultured cells.
167
Cryo-EM structure of oxysterol-bound human Smoothened coupled to a heterotrimeric Gi
TL;DR: 24,25-epoxycholesterol, which is identified as an endogenous ligand of PTCH1, can stimulate Hedgehog signalling in cells and can trigger G-protein signalling via human SMO in vitro, providing molecular insights into Hedgehog signal transduction and the activation of a class-F GPCR.
Structure of human Niemann-Pick C1 protein.
TL;DR: A crystal structure of a large portion of human NPC1 is presented, which reveals the architecture of the SSD, including a cavity that is accessible both vertically to the endosome lumen and laterally to the “luminal” leaflet of the lipid bilayer.
153
Human TRPML1 channel structures in open and closed conformations
TL;DR: The regulatory mechanism of TRPML channels is revealed, the structure of the agonist-binding site is reported, and insights are provided into the molecular basis of mucolipidosis type IV pathogenesis.