Skip to Main content Skip to Navigation
Journal articles

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
Complete list of metadata

https://hal.archives-ouvertes.fr/hal-03219386
Contributor : Florence Vincent Connect in order to contact the contributor
Submitted on : Wednesday, July 7, 2021 - 4:13:42 PM
Last modification on : Tuesday, October 19, 2021 - 10:59:50 PM

Identifiers

  • HAL Id : hal-03219386, version 1

Collections

Citation

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

Share

Metrics

Record views

9