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The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition

Nature Structural Biology volume 3, pages 934939 (1996) | Download Citation

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Abstract

Odorant binding protein (OBP) is the major odorant binding component of mammalian nasal mucosa. The two structures of bovine OBP reported in this paper (one crystallized as purified and one soaked in the presence of a selenium-containing odorant) show that: (i) the OBP dimer is composed of two compact domains related by an approximate two-fold axis of symmetry; (ii) between residues 122 and 123 the polypeptide chains cross from one domain to the other such that each domain is formed by residues from both monomers; (iii) purified OBP already contains two bound odorant molecules (one per monomer)—odorant binding occurs by replacement of these molecules with the added odorant; and (iv) the structure of the odorant binding site can explain OBP's extraordinarily broad odorant specificity.

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Author information

Affiliations

  1. Department of Biophysics and Biophysical Chemistry, University of Pisa, 56124, Pisa, Italy

    • Mario A. Bianchet
    • , Gabrielle Bains
    •  & L. Mario Amzel
  2. Institute of Agricultural Industries, University of Pisa, 56124, Pisa, Italy

    • Paolo Pelosi
  3. Department of Neuroscience, The Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205, USA

    • Jonathan Pevsner
    •  & Solomon H. Snyder
  4. Kennedy Krieger Institute, Baltimore, Maryland 21205, USA

    • Jonathan Pevsner
  5. Department of Genetics, University of Pavia, 27100 Pavia, Italy

    • Hugo L. Monaco
  6. mario@neruda.med.jhu.edu

    • L. Mario Amzel
  7. monaco@ipvgen.unipv.it

    • Hugo L. Monaco

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DOI

https://doi.org/10.1038/nsb1196-934