1e06: Difference between revisions

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[[Image:1e06.gif|left|200px]]
[[Image:1e06.gif|left|200px]]


{{Structure
<!--
|PDB= 1e06 |SIZE=350|CAPTION= <scene name='initialview01'>1e06</scene>, resolution 2.12&Aring;
The line below this paragraph, containing "STRUCTURE_1e06", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:Ipb+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Ipb+Binding+Site+For+Chain+B'>AC2</scene>
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|LIGAND= <scene name='pdbligand=IPB:5-METHYL-2-(1-METHYLETHYL)PHENOL'>IPB</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE=  
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|DOMAIN=
{{STRUCTURE_1e06| PDB=1e06  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e06 OCA], [http://www.ebi.ac.uk/pdbsum/1e06 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e06 RCSB]</span>
}}


'''PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH 5-METHYL-2-(1-METHYLETHYL)PHENOL'''
'''PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH 5-METHYL-2-(1-METHYLETHYL)PHENOL'''
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[[Category: Tegoni, M.]]
[[Category: Tegoni, M.]]
[[Category: Vincent, F.]]
[[Category: Vincent, F.]]
[[Category: lipocalin]]
[[Category: Lipocalin]]
[[Category: odorant binding protein]]
[[Category: Odorant binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:29:40 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:17 2008''

Revision as of 14:29, 2 May 2008

File:1e06.gif

Template:STRUCTURE 1e06

PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH 5-METHYL-2-(1-METHYLETHYL)PHENOL


OverviewOverview

Porcine odorant binding protein (pOBP) is a monomer of 157 amino acid residues, purified in abundance from pig nasal mucosa. In contrast to the observation on lipocalins as retinol binding protein (RBP), major urinary protein (MUP) or bovine odorant binding protein (bOBP), no naturally occurring ligand was found in the beta-barrel cavity of pOBP. Porcine OBP was therefore chosen as a simple model for structure/function studies with odorant molecules. In competition experiments with tritiated pyrazine, the affinity of pOBP towards several odorant molecules belonging to different chemical classes has been found to be of the micromolar order, with a 1:1 stoichiometry. The X-ray structures of pOBP complexed to these molecules were determined at resolution between 2.15 and 1.4 A. As expected, the electron density of the odorant molecules was observed into the hydrophobic beta-barrel of the lipocalin. Inside this cavity, very few specific interactions were established between the odorant molecule and the amino acid side-chains, which did not undergo significant conformational change. The high B-factors observed for the odorant molecules as well as the existence of alternative conformations reveal a non-specific mode of binding of the odorant molecules in the cavity.

About this StructureAbout this Structure

1E06 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

Complexes of porcine odorant binding protein with odorant molecules belonging to different chemical classes., Vincent F, Spinelli S, Ramoni R, Grolli S, Pelosi P, Cambillau C, Tegoni M, J Mol Biol. 2000 Jun 30;300(1):127-39. PMID:10864504 Page seeded by OCA on Fri May 2 14:29:40 2008

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