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Titolo:
THE STRUCTURAL BASIS OF LIPID INTERACTIONS IN LIPOVITELLIN, A SOLUBLELIPOPROTEIN
Autore:
ANDERSON TA; LEVITT DG; BANASZAK LJ;
Indirizzi:
UNIV MINNESOTA,DEPT BIOCHEM,4-225 MILLARD HALL,435 DELAWARE ST SE MINNEAPOLIS MN 55455 UNIV MINNESOTA,DEPT BIOCHEM MINNEAPOLIS MN 55455 UNIV MINNESOTA,DEPT PHYSIOL MINNEAPOLIS MN 55455
Titolo Testata:
Structure
fascicolo: 7, volume: 6, anno: 1998,
pagine: 895 - 909
SICI:
0969-2126(1998)6:7<895:TSBOLI>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRIGLYCERIDE TRANSFER PROTEIN; XENOPUS-LAEVIS; PHOSVITIN COMPLEX; YOLK LIPOPROTEIN; VITELLOGENIN; RESOLUTION; REFINEMENT; SEQUENCE; MAPS; APOLIPOPROTEIN-B-100;
Keywords:
APOLIPOPROTEIN B; LIPOPROTEIN; LIPOVITELLIN; MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN; X-RAY CRYSTALLOGRAPHY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
T.A. Anderson et al., "THE STRUCTURAL BASIS OF LIPID INTERACTIONS IN LIPOVITELLIN, A SOLUBLELIPOPROTEIN", Structure, 6(7), 1998, pp. 895-909

Abstract

Background: The conformation and assembly of lipoproteins, proteins containing large amounts of noncovalently bound lipid, is poorly understood. Lipoproteins present an unusual challenge as they often contain varying loads of lipid and are not readily crystallized. Lipovitellin is a large crystallizable oocyte protein of approximately 1300 residues that contains about 16% w/w lipid. Lipovitellin contains two large domains that appear to be conserved in both microsomal triglyceride transfer protein and apolipoprotein B-100. To gain insight into the conformation of a lipoprotein and the potential modes of binding of both neutral and phospholipid, the crystal structure of lamprey lipovitellin has been determined. Results: We report here the refined crystal structure of lipovitellin at 2.8 Angstrom resolution. The structure contains 1129 amino acid residues located on five peptide chains, one 40-atomphosphatidylcholine, and one 13-atom hydrocarbon chain. The protein contains a funnel-shaped cavity formed primarily by two beta sheets andlined predominantly by hydrophobic residues. Conclusions: Using the crystal structure as a template, a model for the bound lipid is proposed. The lipid-binding cavity is formed primarily by a single-thickness beta-sheet structure which is stabilized by bound lipid. This cavity appears to be flexible, allowing lipid to be loaded or unloaded.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 11:36:12