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Solution structure of FK506-binding protein 12 from Aedes aegypti

Authors

  • Goutam Chakraborty,

    1. Division of Structural Biology and Biochemistry, School of Biological Science, Nanyang Technological University, Singapore 637551
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  • Joon Shin,

    1. Division of Structural Biology and Biochemistry, School of Biological Science, Nanyang Technological University, Singapore 637551
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  • Quoc Toan Nguyen,

    1. Division of Structural Biology and Biochemistry, School of Biological Science, Nanyang Technological University, Singapore 637551
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  • Amaravadhi Harikishore,

    1. Division of Structural Biology and Biochemistry, School of Biological Science, Nanyang Technological University, Singapore 637551
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  • Kwanghee Baek,

    1. Department of Genetic Engineering, College of Life Sciences, Kyung Hee University, Yongin-si, Gyeonggi-do 446-701, Republic of Korea
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  • Ho Sup Yoon

    Corresponding author
    1. Division of Structural Biology and Biochemistry, School of Biological Science, Nanyang Technological University, Singapore 637551
    2. Department of Genetic Engineering, College of Life Sciences, Kyung Hee University, Yongin-si, Gyeonggi-do 446-701, Republic of Korea
    • Division of Structural Biology and Biochemistry, School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551
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Abstract

Dengue remains one of the major public concerns as the virus eludes the immune response. Currently, no vaccines or antiviral therapeutics are available for dengue prevention or treatment. Immunosuppressive drug FK506 shows an antimalarial activity, and its molecular target, FK506-binding protein (FKBP), was identified in human Plasmodium parasites. Likewise, a conserved FKBP family protein has also been identified in Aedes aegypti (AaFKBP12), which is expected to play a similar role in the life cycle of Aedes aegypti, the primary vector of dengue virus infection. As FKBPs belong to a highly conserved class of immunophilin family and are involved in key biological regulations, they are considered as attractive pharmacological targets. In this study, we have determined the nuclear magnetic resonance solution structure of AaFKBP12, a novel FKBP member from Aedes aegypti, and presented its structural features, which may facilitate the design of potential inhibitory ligands against the dengue-transmitting mosquitoes. Proteins 2012;. © 2012 Wiley Periodicals, Inc.

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