1g85
From Proteopedia
CRYSTAL STRUCTURE OF BOVINE ODORANT BINDING PROTEIN COMPLEXED WITH IS NATURAL LIGAND
Overview
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.
About this Structure
1G85 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 17:15:47 2008
