1e06: Difference between revisions
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[[Image:1e06.gif|left|200px]]<br /><applet load="1e06" size=" | [[Image:1e06.gif|left|200px]]<br /><applet load="1e06" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1e06, resolution 2.12Å" /> | caption="1e06, resolution 2.12Å" /> | ||
'''PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH 5-METHYL-2-(1-METHYLETHYL)PHENOL'''<br /> | '''PORCINE ODORANT BINDING PROTEIN COMPLEXED WITH 5-METHYL-2-(1-METHYLETHYL)PHENOL'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1E06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with IPB as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http:// | 1E06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=IPB:'>IPB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E06 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: odorant binding protein]] | [[Category: odorant binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:36:24 2008'' | ||
Revision as of 10:36, 3 February 2008
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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 with as ligand. Known structural/functional Sites: and . 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
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