1obp | pdb_00001obp

ODORANT-BINDING PROTEIN FROM BOVINE NASAL MUCOSA

spinqualitylabelsall models 1obp, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1obp is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: UNX Resources: FirstGlance, OCA, RCSB, PDBsum Function [OBP_BOVIN] This protein binds a wide variety of chemical odorants. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer.,Tegoni M, Ramoni R, Bignetti E, Spinelli S, Cambillau C Nat Struct Biol. 1996 Oct;3(10):863-7. PMID:8836103 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Odorant binding protein

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