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

@article{Tegoni1996DomainSC,
  title={Domain swapping creates a third putative combining site in bovine odorant binding protein dimer},
  author={Mariella Tegoni and Roberto Ramoni and Enrico Bignetti and Silvia Spinelli and Christian Cambillau},
  journal={Nature Structural Biology},
  year={1996},
  volume={3},
  pages={863-867}
}
  • Mariella Tegoni, Roberto Ramoni, +2 authors Christian Cambillau
  • Published in Nature Structural Biology 1996
  • Chemistry, Medicine
  • 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… CONTINUE READING

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