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Domain swapping creates a third putative combining site in bovine odorant binding protein dimer

Nature Structural Biology volume 3, pages 863–867 (1996)Cite this article

Abstract

In mammals, odorant binding proteins may play an important role in the transport of odors towards specific olfactory receptors on sensory neurones across the aqueous compartment of the nasal mucus. We have solved the X-ray structure of such a transport protein, bovine odorant binding protein (OBP) at 2.0 Å resolution. The β-barrel of OBP is similar to that of lipocalins, but OBP dimer association results from domain swapping, an observation unique among the lipocalins. The α-helix of each monomer stacks against the β-barrel of the other monomer. Contrary to previous reports, each monomer has an internal buried cavity which could accommodate a naturally occurring molecule. Besides this cavity, an open cavity is located at the dimer interface. Data in solution suggest that this central cavity may be a binding site created by domain swapping.

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Authors and Affiliations

  1. Architecture et Fonction des Macromolécules Biologiques, UPR9039-CNRS, IFR1, 31 Chemin Joseph Aiguier, 13402, Marseille CEDEX, 20, France

    Mariella Tegoni, Silvia Spinelli & Christian Cambillau

  2. Istituto di Biochimica Veterinaria, Facoltà di Medicina Veterinaria, Università di Parma, Via del Taglio 8, 43100, Parma, Italy

    Roberto Ramoni & Enrico Bignetti

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  1. Mariella Tegoni
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  4. Silvia Spinelli
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  5. Christian Cambillau
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Tegoni, M., Ramoni, R., Bignetti, E. et al. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nat Struct Mol Biol 3, 863–867 (1996). https://doi.org/10.1038/nsb1096-863

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