1A3Y
ODORANT BINDING PROTEIN FROM NASAL MUCOSA OF PIG
Summary for 1A3Y
| Entry DOI | 10.2210/pdb1a3y/pdb |
| Descriptor | ODORANT BINDING PROTEIN (2 entities in total) |
| Functional Keywords | lipocalin, olfaction |
| Biological source | Sus scrofa (pig) |
| Cellular location | Secreted: P81245 |
| Total number of polymer chains | 2 |
| Total formula weight | 33538.96 |
| Authors | Spinelli, S.,Cambillau, C.,Tegoni, M. (deposition date: 1998-01-27, release date: 1999-02-16, Last modification date: 2024-10-30) |
| Primary citation | Spinelli, S.,Ramoni, R.,Grolli, S.,Bonicel, J.,Cambillau, C.,Tegoni, M. The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Biochemistry, 37:7913-7918, 1998 Cited by PubMed Abstract: 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. PubMed: 9609684DOI: 10.1021/bi980179e PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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