Structural and functional aspects of PR-10 proteins

Authors

  • Humberto Fernandes,

    1. Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland
    Current affiliation:
    1. Biophysics Section, Department of Life Sciences, Imperial College, London, UK
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  • Karolina Michalska,

    1. Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Poznan, Poland
    Current affiliation:
    1. Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, Argonne, IL, USA
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  • Michal Sikorski,

    1. Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland
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  • Mariusz Jaskolski

    Corresponding author
    1. Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Poznan, Poland
    • Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland
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Correspondence

M. Jaskolski, Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Grunwaldzka 6, 60-780 Poznan, Poland

Fax: +48 61 8291505

Tel: +48 61 8291274

E-mail: mariuszj@amu.edu.pl

Abstract

Physical, chemical and biological stress factors, such as microbial infection, upregulate the transcription levels of a number of plant genes, coding for the so-called pathogenesis-related (PR) proteins. For PR proteins of class-10 (PR-10), the biological function remains unclear, despite two decades of scientific research. PR-10 proteins have a wide distribution throughout the plant kingdom and the class members share size and secondary structure organization. Throughout the years, we and other groups have determined the structures of a number of PR-10 proteins, both in the crystalline state by X-ray diffraction and in solution by NMR spectroscopy. Despite the accumulating structural information, our understanding of PR-10 function is still limited. PR-10 proteins are rather small (~ 160 amino acids) with a fold consisting of three α helices and seven antiparallel β strands. These structural elements enclose a large hydrophobic cavity that is most probably the key to their functional relevance. Also, the outer surface of these proteins is of extreme interest, as epitopes from a PR-10 subclass cause allergic reactions in humans.

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