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| {{STRUCTURE_1hn2| PDB=1hn2 | SCENE= }} | | {{STRUCTURE_1hn2| PDB=1hn2 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF BOVINE OBP COMPLEXED WITH AMINOANTHRACENE'''
| | ===CRYSTAL STRUCTURE OF BOVINE OBP COMPLEXED WITH AMINOANTHRACENE=== |
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| ==Overview==
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| Bovine 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 line below this paragraph, {{ABSTRACT_PUBMED_11114310}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11114310 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11114310}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Odorant binding protein]] | | [[Category: Odorant binding protein]] |
| [[Category: Olfaction]] | | [[Category: Olfaction]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:01:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:25:11 2008'' |
