Interactions of bile salt micelles and colipase studied through intermolecular nOes
| Autor: | Catherine Chapus, Cyril Dominguez, Brigitte Kerfelec, Corinne Sebban-Kreuzer, Olivier Bornet, Françoise Guerlesquin |
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| Rok vydání: | 2000 |
| Předmět: |
Protein Conformation
Swine Stereochemistry Molecular Sequence Data Molecular Conformation Biophysics Bile salt Colipase Biochemistry Micelle Cofactor Nuclear magnetic resonance Bile Acids and Salts Protein structure Structural Biology Intermolecular nuclear Overhauser effect Genetics Animals Amino Acid Sequence Colipases Horses Nuclear Magnetic Resonance Biomolecular Pancreas Molecular Biology Ternary complex Micelles chemistry.chemical_classification Taurodeoxycholic Acid Sequence Homology Amino Acid biology Intermolecular force Cell Biology Amino acid Folding (chemistry) chemistry biology.protein Sequence Alignment |
| Zdroj: | FEBS Letters. 482:109-112 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(00)02034-2 |
| Popis: | Colipase is a small protein (10 kDa), which acts as a protein cofactor for the pancreatic lipase. Various models of the activated ternary complex (lipase–colipase–bile salt micelles) have been proposed using detergent micelles, but no structural information has been established with bile salt micelles. We have investigated the organization of sodium taurodeoxycholate (NaTDC) micelles and their interactions with pig and horse colipases by homonuclear nuclear magnetic resonance (NMR) spectroscopy. The NMR data supply evidence that the folding of horse colipase is similar to that already described for pig colipase. Intermolecular nuclear Overhauser effects have shown that two conserved aromatic residues interact with NaTDC micelles. |
| Databáze: | OpenAIRE |
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