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1qnd
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The determination of the NMR structure of the sterol carrier protein-2 | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Choinowski, T.]] | [[Category: Choinowski, T.]] | ||
| - | [[Category: Dyer, J | + | [[Category: Dyer, J H.]] |
[[Category: Helmut, H.]] | [[Category: Helmut, H.]] | ||
[[Category: Lopez-Garcia, F.]] | [[Category: Lopez-Garcia, F.]] | ||
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[[Category: sterol carrier protein 2]] | [[Category: sterol carrier protein 2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:39 2008'' |
Revision as of 12:41, 21 February 2008
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STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1QND is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR structure of the sterol carrier protein-2: implications for the biological role., Garcia FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wuthrich K, J Mol Biol. 2000 Jan 21;295(3):595-603. PMID:10623549
Page seeded by OCA on Thu Feb 21 14:41:39 2008
