NMR structure of the sterol carrier protein-2: implications for the biological role
The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone (15)N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for investigations of the mode of action of SCP2. The SCP2 fold is formed by a...
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| Veröffentlicht in: | Journal of molecular biology 2000-01, Vol.295 (3), p.595-603 |
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| container_end_page | 603 |
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| container_issue | 3 |
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| container_title | Journal of molecular biology |
| container_volume | 295 |
| creator | García, F L Szyperski, T Dyer, J H Choinowski, T Seedorf, U Hauser, H Wüthrich, K |
| description | The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone (15)N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for investigations of the mode of action of SCP2. The SCP2 fold is formed by a five-stranded beta-sheet and four alpha-helices. Fatty acid binding to a hydrophobic surface area formed by amino acid residues of the first and third helices, and the beta-sheet, which are all located in the polypeptide segment 8-102, was identified with the use of the spin-labeled substrate 16-doxylstearic acid. In the free protein, the lipid-binding site is covered by the C-terminal segment 105-123, suggesting that this polypeptide segment, which carries the peroxisomal targeting signal (PTS1), might be involved in the regulation of ligand binding. |
| doi_str_mv | 10.1006/jmbi.1999.3355 |
| format | Article |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Carrier Proteins - chemistry Carrier Proteins - metabolism Humans Magnetic Resonance Spectroscopy Models, Molecular Plant Proteins Protein Conformation Protein Folding Rabbits |
| title | NMR structure of the sterol carrier protein-2: implications for the biological role |
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