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Structure of HBP, a multifunctional protein with a serine proteinase fold

Nature Structural Biology volume 4, pages 265–268 (1997)Cite this article

The structure of human heparin binding protein reveals that the serine proteinase fold has been used as a scaffold for a multifunctional protein with antibacterial activity, monocyte and T-cell activating properties and endotoxin and heparin binding capacity.

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Authors and Affiliations

  1. Department of Medicinal Chemistry, Royal Danish School of Pharmacy, Universitetsparken 2, DK-2100, Copenhagen, Denmark

    Lars Fogh Iversen, Jette Sandholm Kastrup & Ingrid Kjøller Larsen

  2. Novo Nordisk A/S, Novo Allé, DK-2880, Bagsvaerd, Denmark

    Søren Erik Bjørn, Poul Baad Rasmussen, Finn Christoph Wiberg & Hans Jacob Flodgaard

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  1. Lars Fogh Iversen
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Iversen, L., Kastrup, J., Bjørn, S. et al. Structure of HBP, a multifunctional protein with a serine proteinase fold. Nat Struct Mol Biol 4, 265–268 (1997). https://doi.org/10.1038/nsb0497-265

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