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Journal Articles Biochemical Journal Year : 2002

Control of domain swapping in bovine odorant-binding protein

Abstract

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 β-barrel to the α-helix. The absence of this residue in OBPb might explain
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Dates and versions

hal-03219386 , version 1 (07-07-2021)

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  • HAL Id : hal-03219386 , version 1

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Roberto Ramoni, Florence Vincent, Alison E Ashcroft, Paolo Accornero, Stefano Grolli, et al.. Control of domain swapping in bovine odorant-binding protein. Biochemical Journal, 2002. ⟨hal-03219386⟩
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