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Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
M Tegoni1, R Ramoni, E Bignetti
1UPR9039-CNRS, IFR1, Marseille, France.
Nature Structural Biology
|October 1, 1996
Summary
Bovine odorant binding proteins (OBPs) transport odorants in the nasal mucus. X-ray structures reveal a unique domain-swapping dimerization mechanism, creating a central cavity potentially involved in odorant binding.
Area of Science:
- Structural Biology
- Biochemistry
- Olfactory Science
Background:
- Odorant binding proteins (OBPs) are crucial for odorant transport in mammalian nasal mucus.
- Understanding OBP structure is key to elucidating olfactory mechanisms.
Purpose of the Study:
- To determine the X-ray structure of bovine odorant binding protein (OBP).
- To investigate the structural basis of OBP dimerization and potential ligand-binding sites.
Main Methods:
- X-ray crystallography at 2.0 Å resolution.
- Structural analysis of bovine OBP.
- Solution-based binding studies.
Main Results:
- The OBP beta-barrel structure resembles lipocalins.
- OBP dimerization occurs via a unique domain-swapping mechanism, where alpha-helices stack against opposing beta-barrels.
- Each monomer possesses an internal cavity, and a novel open cavity exists at the dimer interface, suggested to be a binding site.
Conclusions:
- The domain-swapping dimerization of OBP creates a unique structural feature with a potential ligand-binding site.
- This finding offers new insights into the molecular mechanisms of olfaction and OBP function.