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Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum

Authors

  • Yanan He,

    1. Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland 20850
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  • Yihong Chen,

    1. Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland 20850
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  • Natalia Oganesyan,

    1. Potomac Affinity Proteins, LLC, University of Maryland, Rockville, Maryland 20850
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  • Biao Ruan,

    1. Potomac Affinity Proteins, LLC, University of Maryland, Rockville, Maryland 20850
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  • David O'Brochta,

    1. Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland 20850
    2. Department of Entomology, University of Maryland, Rockville, Maryland 20850
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  • Philip N. Bryan,

    1. Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland 20850
    2. Department of Bioengineering, University of Maryland, Rockville, Maryland 20850
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  • John Orban

    Corresponding author
    1. Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland 20850
    2. Department of Chemistry and Biochemistry, University of Maryland, Rockville, Maryland 20850
    • Institute for Bioscience and Biotechnology Research, and Department of Chemistry and Biochemistry, University of Maryland, 9600 Gudelsky Drive, Rockville, MD 20850
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Abstract

Plasmodium subtilisin 2 (Sub2) is a multidomain protein that plays an important role in malaria infection. Here, we describe the solution NMR structure of a conserved region of the inhibitory prodomain of Sub2 from Plasmodium falciparum, termed prosub2. Despite the absence of any detectable sequence homology, the protozoan prosub2 has structural similarity to bacterial and mammalian subtilisin-like prodomains. Comparison with the three-dimensional structures of these other prodomains suggests a likely binding interface with the catalytic domain of Sub2 and provides insights into the locations of primary and secondary processing sites in Plasmodium prodomains. Proteins 2012;. © 2012 Wiley Periodicals, Inc.

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