NMR structure of the sterol carrier protein-2: implications for the biological role.
Related Articles NMR structure of the sterol carrier protein-2: implications for the biological role.
J Mol Biol. 2000 Jan 21;295(3):595-603
Authors: García FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wüthrich K
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.
PMID: 10623549 [PubMed - indexed for MEDLINE]
Source:
PubMed