1hn2
From Proteopedia
(New page: 200px<br /><applet load="1hn2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hn2, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hn2.gif|left|200px]]<br /><applet load="1hn2" size=" | + | [[Image:1hn2.gif|left|200px]]<br /><applet load="1hn2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hn2, resolution 1.80Å" /> | caption="1hn2, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF BOVINE OBP COMPLEXED WITH AMINOANTHRACENE'''<br /> | '''CRYSTAL STRUCTURE OF BOVINE OBP COMPLEXED WITH AMINOANTHRACENE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bovine odorant-binding protein (bOBP) is a dimeric lipocalin present in | + | 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== | ==About this Structure== | ||
| - | 1HN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ANC and 3OL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ANC:'>ANC</scene> and <scene name='pdbligand=3OL:'>3OL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN2 OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: olfaction]] | [[Category: olfaction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:56 2008'' |
Revision as of 11:02, 21 February 2008
|
CRYSTAL STRUCTURE OF BOVINE OBP COMPLEXED WITH AMINOANTHRACENE
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
1HN2 is a Single protein structure of sequence from Bos taurus with and as ligands. 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 Thu Feb 21 13:02:56 2008
