NMR structure of the sterol carrier protein-2: Implications for the biological role

Francisco López García, Thomas Szyperski, James H. Dyer, Thomas Choinowski, Udo Seedorf, Helmut Hauser, Kurt Wüthrich

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52 Scopus citations


The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone 15N 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.

Original languageEnglish
Pages (from-to)595-603
Number of pages9
JournalJournal of Molecular Biology
Issue number3
StatePublished - 21 Jan 2000


  • NMR
  • Nitroxide spin labels
  • Protein dynamics
  • Protein structure
  • Sterol carrier protein 2


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