Ligand-independent Dimerization of the Extracellular Domain of the Leptin Receptor and Determination of the Stoichiometry of Leptin Binding

• Published in: The Journal of biological chemistry Vol. 272; no. 29; pp. 18304 - 18310
• Main Authors: Devos, René, Guisez, Yves, Van der Heyden, José, White, David W., Kalai, Michael, Fountoulakis, Michael, Plaetinck, Geert
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 18.07.1997; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Animals; Antibodies; BIOCHEMICAL POLYMORPHISM; Carrier Proteins - chemistry; Carrier Proteins - metabolism; Cell Line; COS Cells; Cross-Linking Reagents; Cytoplasm - metabolism; Dimerization; GENERO HUMANO; GENRE HUMAIN; HOMODIMERS; HORMONAS; HORMONE; HORMONE RECEPTORS; HORMONES; Humans; INTERACTIONS; Kinetics; Leptin; MANKIND; Molecular Sequence Data; Obesity; OLIGOMERS; PEPTIDE; Peptide Fragments - chemistry; Peptide Fragments - immunology; PEPTIDES; PEPTIDOS; POLIMORFISMO BIOQUIMICO; POLYMORPHISME BIOCHIMIQUE; POLYPEPTIDES; PROTEINAS RECOMBINANTES; PROTEINE RECOMBINANTE; Proteins - metabolism; RECEPTEUR D'HORMONE; RECEPTORES DE HORMONAS; Receptors, Cell Surface; Receptors, Leptin; RECOMBINANT PROTEINS; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Spodoptera; Transfection

The leptin receptor is a class I transmembrane protein with either a short or a long cytoplasmic domain. Using chemical cross-linking we have analyzed the binding of leptin to its receptor. Cross-linking of radiolabeled leptin to different isoforms of the leptin receptor expressed on COS-1 cells rev...