1g85: Difference between revisions

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New page: left|200px<br /><applet load="1g85" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g85, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1g85.gif|left|200px]]<br /><applet load="1g85" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1g85.gif|left|200px]]<br /><applet load="1g85" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1g85, resolution 1.80&Aring;" />
caption="1g85, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF BOVINE ODORANT BINDING PROTEIN COMPLEXED WITH IS NATURAL LIGAND'''<br />
'''CRYSTAL STRUCTURE OF BOVINE ODORANT BINDING PROTEIN COMPLEXED WITH IS NATURAL LIGAND'''<br />


==Overview==
==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.
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==
1G85 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 3OL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G85 OCA].  
1G85 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=3OL:'>3OL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G85 OCA].  


==Reference==
==Reference==
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[[Category: swapping domain]]
[[Category: swapping domain]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:10 2008''

Revision as of 13:47, 21 February 2008

File:1g85.gif


1g85, resolution 1.80Å

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CRYSTAL STRUCTURE OF BOVINE ODORANT BINDING PROTEIN COMPLEXED WITH IS NATURAL LIGAND

OverviewOverview

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 StructureAbout this Structure

1G85 is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

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