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Titolo:
Vesicle-reconstituted low density lipoprotein receptor - Visualization by cryoelectron microscopy
Autore:
Jeon, H; Shipley, GG;
Indirizzi:
Boston Univ, Sch Med, Ctr Adv Biomed Res, Dept Biophys, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 d Res, Dept Biophys, Boston, MA 02118 USA Boston Univ, Sch Med, Ctr Adv Biomed Res, Dept Biochem, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 d Res, Dept Biochem, Boston, MA 02118 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 39, volume: 275, anno: 2000,
pagine: 30458 - 30464
SICI:
0021-9258(20000929)275:39<30458:VLDLR->2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
COMPLEMENT COMPONENT C9; GROWTH-FACTOR PRECURSOR; CYSTEINE-RICH REPEAT; LDL RECEPTOR; FAMILIAL HYPERCHOLESTEROLEMIA; ELECTRON-MICROSCOPY; 3-DIMENSIONAL STRUCTURE; MEDIATED ENDOCYTOSIS; CYTOPLASMIC DOMAIN; INSULIN-RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Shipley, GG Boston Univ, Sch Med, Ctr Adv Biomed Res, Dept Biophys, 715 Albany St, Boston, MA 02118 USA Boston Univ 715 Albany St Boston MA USA 02118on, MA 02118 USA
Citazione:
H. Jeon e G.G. Shipley, "Vesicle-reconstituted low density lipoprotein receptor - Visualization by cryoelectron microscopy", J BIOL CHEM, 275(39), 2000, pp. 30458-30464

Abstract

The low density lipoprotein (LDL) receptor is a key protein for maintaining cellular cholesterol homeostasis by binding cholesterol-rich lipoproteinsthrough their apoB and apoE apoproteins. The LDL receptor is a transmembrane glycoprotein of M-r similar to 115 kDa; based on its primary sequence, five distinct structural domains have been identified (Yamamoto, T., Davis, C. G., Brown, M. S., Schneider, W. J., Casey, M. L., Goldstein, J. L., and Russell, D. W. (1984) Cell 39, 27-38). As a first step toward providing a structural description of the intact LDL receptor, the receptor has been purified from bovine adrenal cortices, reconstituted into unilamellar egg yolkphosphatidylcholine vesicles, and imaged using cryoelectron microscopy (cryoEM). CryoEM has the advantage of providing images of the reconstituted LDL receptor in its frozen, fully hydrated state. LDL receptor molecules werevisualized as elongated, stick-like projections from the vesicle surface with maximum dimensions similar to 120-Angstrom length by similar to 45-Angstrom width. In some of the images, a short arm (or arms) was visible at thedistal end of the stick-like projections. The LDL receptor was labeled viaaccessible free cysteine residues, probably including that corresponding to Cys-431 of the known full-length sequence of the human LDL receptor. The accessible cysteine was demonstrated using a maleimide-biotin streptavidin conjugate and confirmed by labeling with monomaleimido-Nanogold. Images obtained by cryoEM showed that the extracellular stick-like domain of the reconstituted LDL receptor was labeled by Nanogold. This combined cryoEM-Nanogold labeling study has provided the first low resolution structural images of the reconstituted, full-length bovine LDL receptor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:28:32