NMR structure of the sterol carrier protein-2: implications for the biological role.
J Mol Biol
; 295(3): 595-603, 2000 Jan 21.
Article
em En
| MEDLINE
| ID: mdl-10623549
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.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Proteínas de Transporte
Limite:
Animals
/
Humans
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Suíça