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Titolo:
A mechanism of membrane neutral lipid acquisition by the microsomal triglyceride transfer protein
Autore:
Read, J; Anderson, TA; Ritchie, PJ; Vanloo, B; Amey, J; Levitt, D; Rosseneu, M; Scott, J; Shoulders, CC;
Indirizzi:
Hammersmith Hosp, Imperial Coll, Sch Med, Mol Med Grp,MRC,Clin Sci Ctr, London W12 0NN, England Hammersmith Hosp London England W12 0NN Sci Ctr, London W12 0NN, England Hammersmith Hosp, Imperial Coll, Sch Med, Natl Heart & Lung Inst, London W12 0NN, England Hammersmith Hosp London England W12 0NN ng Inst, London W12 0NN, England Univ Minnesota, Sch Med, Dept Biochem, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 iochem, Minneapolis, MN 55455 USA State Univ Ghent, Dept Biochem, Lab Lipoprot Chem, B-9000 Ghent, Belgium State Univ Ghent Ghent Belgium B-9000 poprot Chem, B-9000 Ghent, Belgium
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 39, volume: 275, anno: 2000,
pagine: 30372 - 30377
SICI:
0021-9258(20000929)275:39<30372:AMOMNL>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PEPTIDES; BINDING; ABETALIPOPROTEINEMIA; LIPOVITELLIN; LIPOPROTEINS; TRANSPORT; LOCATION; VARIANT; FUSION; MODELS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Shoulders, CC Hammersmith Hosp, Imperial Coll, Sch Med, Mol Med Grp,MRC,Clin Sci Ctr, DuCane Rd, London W12 0NN, England Hammersmith Hosp Du Cane Rd London England W12 0NN England
Citazione:
J. Read et al., "A mechanism of membrane neutral lipid acquisition by the microsomal triglyceride transfer protein", J BIOL CHEM, 275(39), 2000, pp. 30372-30377

Abstract

The microsomal triglyceride transfer protein (MTP) and apolipoprotein B (apoB) belong to the vitellogenin (VTG) family of lipid transfer proteins. MTP is essential for the intracellular assembly and secretion of apoB-containing lipoproteins, the key intravascular lipid transport proteins in vertebrates. We report the predicted three-dimensional structure of the C-terminallipid binding cavity of MTP, modeled on the crystal structure of the lamprey VTG gene product, lipovitellin. The cavity in MTP resembles those found in the intracellular lipid-binding proteins and bactericidal/permeability-increasing protein. Two conserved helices, designated A and B, at the entrance to the MTP cavity mediate lipid acquisition and binding. Helix A (amino acids 725-736) interacts with membranes in a manner similar to viral fusionpeptides. Mutation of helix A blocks the interaction of MTP with phospholipid vesicles containing triglyceride and impairs triglyceride binding. Mutations of helix B (amino acids 781-786) and of N780Y, which causes abetalipoproteinemia, have no impact on the interaction of MTP with phospholipid vesicles but impair triglyceride binding. We propose that insertion of helix Ainto lipid membranes is necessary for the acquisition of neutral lipids and that helix B is required for their transfer to the lipid binding cavity of MTP.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 07:19:50