1g85: Difference between revisions
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[[Image:1g85.gif|left|200px]] | [[Image:1g85.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF BOVINE ODORANT BINDING PROTEIN COMPLEXED WITH IS NATURAL LIGAND''' | {{Structure | ||
|PDB= 1g85 |SIZE=350|CAPTION= <scene name='initialview01'>1g85</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=3OL:1-OCTEN-3-OL'>3OL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF BOVINE ODORANT BINDING PROTEIN COMPLEXED WITH IS NATURAL LIGAND''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1G85 is a [ | 1G85 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G85 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11114310 11114310] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: swapping domain]] | [[Category: swapping domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:19:31 2008'' | ||
Revision as of 12:19, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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