ArticleThe Biochemical journal2002
Control of domain swapping in bovine odorant-binding protein.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 62 citations in OpenAlex.
- OBP-functionalized/hybrid superparamagnetic nanoparticles forRSC advances · 2021Article
- Vertebrate odorant binding proteins as antimicrobial humoral components of innate immunity for pathogenic microorganisms.PloS one · 2019Article
- Article
- Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway.Scientific reports · 2016Article
- Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms.PeerJ · 2016Article
- Article
- Energy transfer studies between Trp residues of three lipocalin proteins family, α1-acid glycoprotein, (orosomucoid), β-lactoglobulin and porcine odorant binding protein and the fluorescent probe, 1-aminoanthracene (1-AMA).Journal of fluorescence · 2015Article
- The quaternary structure of the recombinant bovine odorant-binding protein is modulated by chemical denaturants.PloS one · 2014Article
- NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping.PloS one · 2012Article
- Article
- Characterization of a deswapped triple mutant bovine odorant binding protein.International journal of molecular sciences · 2011Article
- Effect of 1-aminoanthracene (1-AMA) binding on the structure of three lipocalin proteins, the dimeric β lactoglobulin, the dimeric odorant binding protein and the monomeric α1-acid glycoprotein. Fluorescence spectra and lifetimes studies.Journal of fluorescence · 2010Article
- Insights into Protein Sequence and Structure-Derived Features Mediating 3D Domain Swapping Mechanism using Support Vector Machine Based Approach.Bioinformatics and biology insights · 2010Article
- The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids.FEBS letters · 2006Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As revealed by the X-ray structure, bovine odorant-binding protein (OBPb) is a domain swapped dimer [Tegoni, Ramoni, Bignetti, Spinelli and Cambillau (1996) Nat. Struct. Biol. 3, 863-867; Bianchet, Bains, Petosi, Pevsner, Snyder, Monaco and Amzel (1996) Nat. Struct. Biol. 3, 934-939]. This contrasts with all known mammalian OBPs, which are monomers, and in particular with porcine OBP (OBPp), sharing 42.3% identity with OBPb. By the mechanism of domain swapping, monomers are proposed to evolve into dimers and oligomers, as observed in human prion. Comparison of bovine and porcine OBP sequences pointed at OBPp glycine 121, in the hinge linking the beta-barrel to the alpha-helix. The absence of this residue in OBPb might explain why the normal lipocalin beta-turn is not formed. In order to decipher the domain swapping determinants we have produced a mutant of OBPb in which a glycine residue was inserted after position 121, and a mutant of OBPp in which glycine 121 was deleted. The latter mutation did not result in dimerization, while OBPb-121Gly+ became monomeric, suggesting that domain swapping was reversed. Careful structural analysis revealed that besides the presence of a glycine in the hinge, the dimer interface formed by the C-termini and by the presence of the lipocalins conserved disulphide bridge may also control domain swapping.
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