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From Proteopedia
CRYSTAL STRUCTURE OF BOVINE OBP COMPLEXED WITH AMINOANTHRACENE
Structural highlights
FunctionOBP_BOVIN This protein binds a wide variety of chemical odorants. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBovine odorant-binding protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-A resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet et al. (1996) Nat. Struct. Biol. 3, 934-939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-A resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body emanations of humans and animals. The compound 1-octen-3-ol is also an extremely potent olfactory attractant for many insect species, including some parasite vectors like Anopheles (Plasmodium) or Glossina (Trypanosoma). For the first time, a function can be assigned to an OBP, with a possible role of bOBP in the ecological relationships between bovine and insect species. The insect attractant 1-octen-3-ol is the natural ligand of bovine odorant-binding protein.,Ramoni R, Vincent F, Grolli S, Conti V, Malosse C, Boyer FD, Nagnan-Le Meillour P, Spinelli S, Cambillau C, Tegoni M J Biol Chem. 2001 Mar 9;276(10):7150-5. Epub 2000 Dec 12. PMID:11114310[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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