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 ... [(full description)]
About this StructureAbout this Structure
1E06 is a [Single protein] structure of sequence from [Sus scrofa] with IPB as [ligand]. Structure known Active Sites: AC1 and AC2. 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 Tue Oct 30 15:03:35 2007