1a3y
From Proteopedia
| |||||||
| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ODORANT BINDING PROTEIN FROM NASAL MUCOSA OF PIG
Overview
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 Structure
1A3Y is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 18:32:44 2008
