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Dong, Xianchi

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Dong

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Xianchi

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Dong, Xianchi
Author's Publications: search.filters.isAuthorOfPublication.b76a4880-0da1-43c1-9548-405dc6dc78ed

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    Prodomain–growth factor swapping in the structure of pro-TGF-β1
    (American Society for Biochemistry and Molecular Biology, 2018) Zhao, Bo; Xu, Shutong; Dong, Xianchi; Lu, Chafen; Springer, Timothy
    TGF-β is synthesized as a proprotein that dimerizes in the endoplasmic reticulum. After processing in the Golgi to cleave the N-terminal prodomain from the C-terminal growth factor (GF) domain in each monomer, pro-TGF-β is secreted and stored in latent complexes. It is unclear which prodomain and GF monomer are linked before proprotein convertase cleavage and how much conformational change occurs following cleavage. We have determined a structure of pro-TGF-β1 with the proprotein convertase cleavage site mutated to mimic the structure of the TGF-β1 proprotein. Structure, mutation, and model building demonstrate that the prodomain arm domain in one monomer is linked to the GF that interacts with the arm domain in the other monomer in the dimeric structure (i.e. the prodomain arm domain and GF domain in each monomer are swapped). Swapping has important implications for the mechanism of biosynthesis in the TGF-β family and is relevant to the mechanism for preferential formation of heterodimers over homodimers for some members of the TGF-β family. Our structure, together with two previous ones, also provides insights into which regions of the prodomain–GF complex are highly structurally conserved and which are perturbed by crystal lattice contacts.
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    Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus
    (Nature Publishing Group, 2017) Kotecha, Abhay; Wang, Quan; Dong, Xianchi; Ilca, Serban L.; Ondiviela, Marina; Zihe, Rao; Seago, Julian; Charleston, Bryan; Fry, Elizabeth E.; Abrescia, Nicola G. A.; Springer, Timothy; Huiskonen, Juha T.; Stuart, David I.
    Foot-and-mouth disease virus (FMDV) mediates cell entry by attachment to an integrin receptor, generally αvβ6, via a conserved arginine–glycine–aspartic acid (RGD) motif in the exposed, antigenic, GH loop of capsid protein VP1. Infection can also occur in tissue culture adapted virus in the absence of integrin via acquired basic mutations interacting with heparin sulphate (HS); this virus is attenuated in natural infections. HS interaction has been visualized at a conserved site in two serotypes suggesting a propensity for sulfated-sugar binding. Here we determined the interaction between αvβ6 and two tissue culture adapted FMDV strains by cryo-electron microscopy. In the preferred mode of engagement, the fully open form of the integrin, hitherto unseen at high resolution, attaches to an extended GH loop via interactions with the RGD motif plus downstream hydrophobic residues. In addition, an N-linked sugar of the integrin attaches to the previously identified HS binding site, suggesting a functional role.