Odorant binding initially occurring at the central pocket in bovine odorant-binding protein

Why bovine odorant-binding protein (OBPb), among OBP family, assumes a dimeric structure has been unclear. Here we clarified, by measuring the fluorescence of intrinsic tryptophan and tyrosine residues of intact OBPb and OBPb whose C-terminal 10 amino acids were deleted, that odorant enters the cent...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-08, Vol.333 (4), p.1227-1233
Main Authors: Ikematsu, Mineo, Takaoka, Daizo, Yasuda, Masashi
Format: Article
Language:English
Subjects:
Animals
Anthracenes - analysis
Anthracenes - chemistry
Binding Sites
Cattle
Central pocket
Dimeric structure
Dimerization
Domain swapping
Internal cavity
Odorant-binding protein
Odorants - analysis
Protein Binding
Protein Conformation
Receptors, Odorant - analysis
Receptors, Odorant - chemistry
Structure-Activity Relationship
Terpenes - analysis
Terpenes - chemistry
Tryptophan - chemistry
Tryptophan fluorescence
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Description
Summary:Why bovine odorant-binding protein (OBPb), among OBP family, assumes a dimeric structure has been unclear. Here we clarified, by measuring the fluorescence of intrinsic tryptophan and tyrosine residues of intact OBPb and OBPb whose C-terminal 10 amino acids were deleted, that odorant enters the central pocket formed by the dimerization when OBPb first encounters odorant, and odorant with high affinity with OBPb subsequently enters the internal cavity (suggested binding site), releasing the pre-bound odorant. The internal cavity-bound odorant can be released by the binding of other odorants at another internal cavity or at the central pocket, depending on the binding odorants. Due to this mechanism enabled by the dimerization, OBPb is more reactive than other monomeric OBPs.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2005.06.031