NMR Structure of the Sterol Carrier Protein-2Implications 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 five-stranded β-sheet and four α-helices. Fatty acid binding to a hydrophobic surface area formed by amino acid residues of the first and third helices, and the β-sheet, which are all located in the polypeptide segment 8-102, was identified with the use of the spinlabeled 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. (C) 2000 Academic Press.
MSU Digital Commons Citation
García, Francisco López; Szyperski, Thomas; Dyer, Jim; Choinowski, Thomas; Seedorf, Udo; Hauser, Helmut; and Wüthrich, Kurt, "NMR Structure of the Sterol Carrier Protein-2Implications for the Biological Role" (2000). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 10.