title: Recombinant expression and partial characterization of the human formyl peptide receptor.
abstract: FMLP-receptor DNA was expressed in Escherichia coli. The expressed product could specifically bind FMLP. This is the first-reported expression of a functional FMLP receptor in Escherichia coli. We confirm that receptor glycosylation is not essential for ligand binding. A deletion mutant did not bind FMLP, suggesting that the deleted portion plays a role in ligand binding.
authors.affiliation: Department of Oral Biology, School of Dentistry, State University of New York at Buffalo 14214.
authors.forename: A
authors.initials: A
authors.lastname: Lala
authors.forename: A
authors.initials: A
authors.lastname: Sharma
authors.forename: H T
authors.initials: HT
authors.lastname: Sojar
authors.forename: S J
authors.initials: SJ
authors.lastname: Radel
authors.forename: R J
authors.initials: RJ
authors.lastname: Genco
authors.forename: E
authors.initials: E
authors.lastname: De Nardin
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D044042:Receptors, Formyl Peptide; D011971:Receptors, Immunologic / Q000096:biosynthesis* / Q000737:chemistry; D011994:Recombinant Proteins / Q000096:biosynthesis*
chemical_list: D044042:Receptors, Formyl Peptide; D011971:Receptors, Immunologic; D011994:Recombinant Proteins