title: Is asparagine deamidation in the porcine odorant-binding protein related to the odor molecules binding?
abstract: Odorant-binding proteins are biomolecules belonging to the lipocalin family. Among all the odorant-binding proteins, the porcine odorant-binding protein has been well characterized. This protein is a monomer that is characterized by the presence of the beta-barrel structure and of the disulphide bridge. The internal cavity of the beta-barrel is the binding site. In this study we have investigated the structural properties of the porcine odorant-binding protein by mass spectrometry experiments. Our data allow us to hypothesize that specific deamidation mechanisms of specific amino acid residues can be responsible for the binding properties of this class of proteins.
authors.affiliation: Proteomic and Biomolecular Mass, Spectrometry Centre, ISA-CNR, Avellino, Italy.
authors.forename: Gianfranco
authors.initials: G
authors.lastname: Mamone
authors.forename: Sabato
authors.initials: S
authors.lastname: D'Auria
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001216:Asparagine / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D054834:Lipocalins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009297:Nasal Mucosa / Q000201:enzymology / Q000502:physiology; D009812:Odorants; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D018035:Receptors, Odorant / Q000737:chemistry* / Q000378:metabolism*; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D034421:Sus scrofa; D053719:Tandem Mass Spectrometry
chemical_list: D054834:Lipocalins; D018035:Receptors, Odorant; C045648:odorant-binding protein; D001216:Asparagine; D000581:Amidohydrolases