1OBP
ODORANT-BINDING PROTEIN FROM BOVINE NASAL MUCOSA
Summary for 1OBP
| Entry DOI | 10.2210/pdb1obp/pdb |
| Descriptor | ODORANT-BINDING PROTEIN, UNKNOWN ATOM OR ION (3 entities in total) |
| Functional Keywords | olfaction, nose, transport, lipocalin, odorant-binding protein |
| Biological source | Bos taurus (cattle) |
| Cellular location | Secreted: P07435 |
| Total number of polymer chains | 2 |
| Total formula weight | 36914.61 |
| Authors | Tegoni, M.,Cambillau, C. (deposition date: 1996-01-14, release date: 1996-10-14, Last modification date: 2024-02-14) |
| Primary citation | Tegoni, M.,Ramoni, R.,Bignetti, E.,Spinelli, S.,Cambillau, C. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer Nat.Struct.Biol., 3:863-867, 1996 Cited by PubMed Abstract: In mammals, odorant binding proteins may play an important role in the transport of odors towards specific olfactory receptors on sensory neurones across the aqueous compartment of the nasal mucus. We have solved the X-ray structure of such a transport protein, bovine odorant binding protein (OBP) at 2.0 A resolution. The beta-barrel of OBP is similar to that of lipocalins, but OBP dimer association results from domain swapping, an observation unique among the lipocalins. The alpha-helix of each monomer stacks against the beta-barrel of the other monomer. Contrary to previous reports, each monomer has an internal buried cavity which could accommodate a naturally occurring molecule. Besides this cavity, an open cavity is located at the dimer interface. Data in solution suggest that this central cavity may be a binding site created by domain swapping. PubMed: 8836103DOI: 10.1038/nsb1096-863 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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