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http://purl.uniprot.org/citations/8269963http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8269963http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8269963http://www.w3.org/2000/01/rdf-schema#comment"Boar spermadhesins AQN-1, AQN-3 and AWN form a recently described protein family, synthesized by the sexual accessory glands, and become associated with the sperm head upon ejaculation. They contain 109-133 amino acid residues, two conserved disulphide bridges, are not glycosylated, and have 40-60% primary structure identity. These boar polypeptides are multifunctional proteins, which possess heparin-, serine-protease-inhibitor-and/or zona-pellucida-glycoprotein-binding capability and have, therefore, been implicated in sperm capacitation and sperm-oocyte attachment. AQN-2 (18-20 kDa), however, is unique among boar spermadhesins in that it is the only member of the family which is known to be glycosylated and which possesses weak zona-pellucida-binding but not seminal-plasma-inhibitor-binding ability. In this study we report the structural and functional characterization of the two glycoproteins contained in the AQN-2 fraction. One component is identical with PSP-I, a major porcine seminal plasma protein whose function has not yet been identified, while the second protein is a glycosylated isoform of AQN-3. Here we show that the inability of the glycosylated boar spermadhesins to bind seminal-plasma protease inhibitors as well as the weak binding of glycosylated AQN-3 to zona pellucida glycoproteins is due to the presence of the oligosacharide chain on a conserved asparagine residue. This indicates that modification of a spermadhesin polypeptide framework may serve to modulate its ligand-binding capabilities."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1993.tb18426.x"xsd:string
http://purl.uniprot.org/citations/8269963http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1993.tb18426.x"xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Calvete J.J."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Calvete J.J."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Sanz L."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Sanz L."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Mann K."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Mann K."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Schaefer W."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Schaefer W."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Toepfer-Petersen E."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Toepfer-Petersen E."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Diaz-Maurino T."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Diaz-Maurino T."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Solis D."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/author"Solis D."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/pages"719-725"xsd:string
http://purl.uniprot.org/citations/8269963http://purl.uniprot.org/core/pages"719-725"xsd:string