Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain-swapped dimer

Authors

  • Masamichi Nagae,

    1. Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, Saitama, Japan
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  • Akemi Ikeda,

    1. Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, Saitama, Japan
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  • Yu Kitago,

    1. Institute for Protein Research, Osaka University, Osaka, Japan
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  • Naoki Matsumoto,

    1. Department of Integrated Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan
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  • Kazuo Yamamoto,

    1. Department of Integrated Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan
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  • Yoshiki Yamaguchi

    Corresponding author
    1. Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, Saitama, Japan
    • Correspondence to: Yoshiki Yamaguchi, Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. E-mail: yyoshiki@riken.jp

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ABSTRACT

We report on crystal structures of a carbohydrate recognition domain (CRD) of human C-type lectin receptor blood dendritic cell antigen-2 (BDCA2). Three different crystal forms were obtained at 1.8–2.3 Å resolution. In all three, the CRD has a basic C-type lectin fold, but a long loop extends away from the core domain to form a domain-swapped dimer. The structures of the dimers from the three different crystal forms superimpose well, indicating that domain swapping and dimer formation are energetically stable. The structure of the dimer is compared with other domain-swapped proteins, and a possible regulation mechanism of BDCA2 is discussed. Proteins 2014; 82:1512–1518. © 2013 Wiley Periodicals, Inc.

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