1QND

STEROL CARRIER PROTEIN-2, NMR, 20 STRUCTURES

Summary for 1QND

• Entry DOI: 10.2210/pdb1qnd/pdb
• Descriptor: NONSPECIFIC LIPID-TRANSFER PROTEIN (1 entity in total)
• Functional Keywords: transfer protein, sterol carrier protein 2, protein structure, protein dynamics, nitroxide spin labels, lipid binding
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm. Isoform SCPx: Peroxisome. Isoform SCP2: Mitochondrion (Probable): P22307
• Total number of polymer chains: 1
• Total formula weight: 13260.34

Authors

Lopez-Garcia, F.,Szyperski, T.,Dyer, J.H.,Choinowski, T.,Seedorf, U.,Hauser, H.,Wuthrich, K. (deposition date: 1999-10-14, release date: 2000-07-03, Last modification date: 2024-05-15)

Primary citation

Lopez-Garcia, F.,Szyperski, T.,Dyer, J.H.,Choinowski, T.,Seedorf, U.,Hauser, H.,Wuthrich, K.
NMR Structure of the Sterol Carrier Protein-2: Implications for the Biological Role
J.Mol.Biol., 295:595-, 2000

PubMed Abstract: 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.

PubMed: 10623549
DOI: 10.1006/JMBI.1999.3355

Experimental method

SOLUTION NMR