1a3y
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ODORANT BINDING PROTEIN FROM NASAL MUCOSA OF PIG
OverviewOverview
The X-ray structure of the porcine odorant binding protein (OBPp) was, determined at 2.25 A resolution. This lipocalin is a monomer and is devoid, of naturally occurring bound ligand, contrary to what was observed in the, case of bovine OBP [Tegoni, M., et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet, M. A., et al. (1996) Nat. Struct. Biol. 3, 934-939]. In, this latter protein, a dimer without any disulfide bridges, domain, swapping was found to occur between the beta- and alpha-domains. A single, Gly (121) insertion was found in OBPp when it was compared to OBPb, which, may prevent domain swapping from taking place. The presence of a disulfide, bridge between the OBPp beta- and alpha-domains (cysteines 63 and 155) may, lock the resulting fold in a nonswapped monomeric conformation., Comparisons with other OBPs indicate that the two cysteines involved in, the OBPp disulfide bridge are conserved in the sequence, suggesting that, OBPp may be considered a prototypic OBP fold, and not OBPb.
About this StructureAbout this Structure
1A3Y is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism., Spinelli S, Ramoni R, Grolli S, Bonicel J, Cambillau C, Tegoni M, Biochemistry. 1998 Jun 2;37(22):7913-8. PMID:9609684
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