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Solution structure of the SH3 domain of DOCK180

Authors

  • Xiangrong Liu,

    1. Key Laboratory of Molecular Medicine, Ministry of Education, Department of Biochemistry and Molecular Biology, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, People's Republic of China
    2. School of Life Sciences, Fudan University, Shanghai, People's Republic of China
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  • Fengjuan Li,

    1. Key Laboratory of Molecular Medicine, Ministry of Education, Department of Biochemistry and Molecular Biology, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, People's Republic of China
    2. Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Department of Chemistry, Fudan University, Shanghai, People's Republic of China
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    • Xiangrong Liu and Fengjuan Li contributed equally to this work.

  • Zhu Pan,

    1. Key Laboratory of Molecular Medicine, Ministry of Education, Department of Biochemistry and Molecular Biology, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, People's Republic of China
    2. Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Department of Chemistry, Fudan University, Shanghai, People's Republic of China
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  • Wenning Wang,

    Corresponding author
    1. Key Laboratory of Molecular Medicine, Ministry of Education, Department of Biochemistry and Molecular Biology, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, People's Republic of China
    2. Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Department of Chemistry, Fudan University, Shanghai, People's Republic of China
    • Department of Chemistry, Fudan University, 220 Handan Road, Shanghai 200433, People's Republic of China & Email; or Wenyu Wen, Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, 131 Dong An Road, Shanghai 200032, People's Republic of China
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  • Wenyu Wen

    Corresponding author
    1. Key Laboratory of Molecular Medicine, Ministry of Education, Department of Biochemistry and Molecular Biology, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, People's Republic of China
    2. School of Life Sciences, Fudan University, Shanghai, People's Republic of China
    • Institutes of Biomedical Sciences, Fudan University, 131 Dong An Road, Shanghai 200032, People's Republic of China
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Abstract

DOCK180 family proteins are Rho guanine nucleotide exchange factors. DOCK1-5 contains an N-terminal SH3 domain implicated in their autoinhibition. Release of the closed conformation requires the interaction between SH3 and engulfment and cell motility (ELMO). Here, we solved the solution structure of DOCK180 SH3 domain, which shares similar target binding features with the SH3 domain of DOCK2. The conserved N-terminal extension packs with the SH3 core domain and forms a new target binding site distinct from the canonical “PxxP” site. Our results demonstrate that the bidentate target binding mode of DOCK180 SH3 domain might be a general feature in all DOCK proteins. Proteins 2013. © 2012 Wiley Periodicals, Inc.

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