1qnd: Difference between revisions

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==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.

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==

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[[Category: Single protein]]

[[Category: Choinowski, T.]]

[[Category: Dyer, J.H.]]

[[Category: Dyer, J H.]]

[[Category: Helmut, H.]]

[[Category: Lopez-Garcia, F.]]

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[[Category: sterol carrier protein 2]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Choinowski, T.]]
-[[Category: Dyer, J.H.]]
+[[Category: Dyer, J H.]]
 [[Category: Helmut, H.]]
 [[Category: Lopez-Garcia, F.]]
@@ Line 26: / Line 26: @@
 [[Category: sterol carrier protein 2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:45:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:39 2008''