Structural highlights
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
Odorant binding protein (OBP) is the major odorant binding component of mammalian nasal mucosa. The two structures of bovine OBP reported in this paper (one crystallized as purified and one soaked in the presence of a selenium-containing odorant) show that: (i) the OBP dimer is composed of two compact domains related by an approximate two-fold axis of symmetry; (ii) between residues 122 and 123 the polypeptide chains cross from one domain to the other such that each domain is formed by residues from both monomers; (iii) purified OBP already contains two bound odorant molecules (one per monomer)-odorant binding occurs by replacement of these molecules with the added odorant; and (iv) the structure of the odorant binding site can explain OBP's extraordinarily broad odorant specificity.
The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition.,Bianchet MA, Bains G, Pelosi P, Pevsner J, Snyder SH, Monaco HL, Amzel LM Nat Struct Biol. 1996 Nov;3(11):934-9. PMID:8901871[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bianchet MA, Bains G, Pelosi P, Pevsner J, Snyder SH, Monaco HL, Amzel LM. The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition. Nat Struct Biol. 1996 Nov;3(11):934-9. PMID:8901871
