Molecular interactions between human lactotransferrin and the phytohemagglutinin-activated human lymphocyte lactotransferrin receptor lie in two loop-containing regions of the N-terminal domain I of human lactotransferrin
| Autor: | Dominique Legrand, Gérard Vergoten, Joël Mazurier, Geneviève Spik, Pierrette Maes, Elisabeth Rochard, Jean Montreuil, Abdelaziz Elass |
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| Přispěvatelé: | Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 1992 |
| Předmět: |
Models
Molecular Protein Conformation Peptide MESH: Amino Acid Sequence Lymphocyte Activation Biochemistry chemistry.chemical_compound Protein structure MESH: Protein Conformation Lymphocytes Fluorescein isothiocyanate MESH: Peptide Fragments Peptide sequence Cells Cultured Chromatography High Pressure Liquid MESH: Receptors Cell Surface chemistry.chemical_classification 0303 health sciences MESH: Kinetics MESH: Molecular Weight 030302 biochemistry & molecular biology Lactotransferrin Fluorescein-5-isothiocyanate MESH: Models Molecular MESH: Cells Cultured Molecular Sequence Data Receptors Cell Surface MESH: Binding Competitive Biology Binding Competitive MESH: Phytohemagglutinins 03 medical and health sciences MESH: Fluorescein-5-isothiocyanate Cell surface receptor Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Phytohemagglutinins Binding site MESH: Chromatography High Pressure Liquid MESH: Lymphocyte Activation 030304 developmental biology MESH: Molecular Sequence Data MESH: Humans Peptide Fragments MESH: Lactoferrin Molecular Weight Kinetics Lactoferrin chemistry Transferrin MESH: Lymphocytes |
| Zdroj: | Biochemistry Biochemistry, American Chemical Society, 1992, 31 (38), pp.9243-51 Biochemistry, 1992, 31 (38), pp.9243-51 |
| ISSN: | 0006-2960 1520-4995 |
| Popis: | International audience; Fluorescein isothiocyanate derivatization of the human lactotransferrin on Lys-264 inhibits the binding of the protein of human PHA-activated lymphocytes [Legrand, D., Mazurier, J., Maes, P., Rochard, E., Montreuil, J., & Spik, G. (1991) Biochem. J. 276, 733-738], indicating that part of the receptor-binding site is located in the N-terminal domain I of lactotransferrin. In the present study, a 6-kDa peptide (residues 4-52) was isolated from the N-terminal lobe of human lactotransferrin which inhibited the binding of the protein to its cell receptor. In addition, lactotransferrin was derivatized using sulfosuccinimidyl 2-(p-azidosalicylamido)ethyl-1,3'-dithiopropionate (SASD) and sulfosuccinimidyl 6-((4'-azido-2'-nitrophenyl)amino)hexanoate (sulfo-SANPAH), two heterobifunctional reagents generally used for receptor-ligand cross-linking. The azide group of these two reagents was inactivated by photolysis, and only the succinimidyl ester group was allowed to react with lysine residues of the protein. The binding of the derivatized lactotransferrins to the human lymphocyte receptor was assayed. SASD, which binds to Lys-74, was able to inhibit the binding of lactotransferrin to the cell receptor, in contrast to Lys-281-binding sulfo-SANPAH. Molecular modeling showed the position of SASD, sulfo-SANPAH, and fluorescein molecules at the surface of the protein and suggested that SASD and fluorescein could mask residues 4-6 and two loop-containing regions of human lactotransferrin (residues 28-34 and 38-45). The comparison of the primary and tertiary structures of human lactotransferrin and serotransferrin, which bind to specific cell receptors, shows that the above-mentioned regions, which are likely involved in protein-receptor interactions, possess specific structural features. |
| Databáze: | OpenAIRE |
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