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Titolo:
BINDING OF MONOCLONAL-ANTIBODIES AGAINST THE CARBOXYL-TERMINAL SEGMENT OF THE NICOTINIC RECEPTOR DELTA-SUBUNIT SUGGESTS AN UNUSUAL TRANSMEMBRANE DISPOSITION OF THIS SEQUENCE REGION
Autore:
LEI SJ; OKITA DK; CONTIFINE BM;
Indirizzi:
UNIV MINNESOTA,DEPT BIOCHEM,1479 GORTNER AVE ST PAUL MN 55108 UNIV MINNESOTA,DEPT BIOCHEM ST PAUL MN 55108 UNIV MINNESOTA,DEPT PHARMACOL MINNEAPOLIS MN 55455
Titolo Testata:
Biochemistry
fascicolo: 20, volume: 34, anno: 1995,
pagine: 6675 - 6688
SICI:
0006-2960(1995)34:20<6675:BOMATC>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
SODIUM DODECYL-SULFATE; TORPEDO ACETYLCHOLINE-RECEPTOR; HIGH-AFFINITY BINDING; GATED ION CHANNELS; ALPHA-SUBUNIT; IMMUNOCHEMICAL TESTS; AMINO-ACIDS; PROTEINS; MEMBRANE; CALIFORNICA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
62
Recensione:
Indirizzi per estratti:
Citazione:
S.J. Lei et al., "BINDING OF MONOCLONAL-ANTIBODIES AGAINST THE CARBOXYL-TERMINAL SEGMENT OF THE NICOTINIC RECEPTOR DELTA-SUBUNIT SUGGESTS AN UNUSUAL TRANSMEMBRANE DISPOSITION OF THIS SEQUENCE REGION", Biochemistry, 34(20), 1995, pp. 6675-6688

Abstract

Monoclonal antibodies (mAbs) specific for the carboxyl terminal region of the delta subunit of Torpedo nicotinic acetylcholine receptor (AChR), derived from mice immunized with AChR or a synthetic carboxyl terminal sequence of the delta subunit (C delta-mAbs), were used to determine the transmembrane disposition of their epitope(s) by immunoelectron microscopy, using AChR-rich postsynaptic membrane fragments from Torpedo electroplax. Some C delta-mAbs recognized only the cytoplasmic side of the membranes, some both sides to a similar extent, and others bound mostly, but not exclusively, to the cytoplasmic side. Binding ofC delta-mAbs to the membranes was specifically blocked by synthetic peptides containing the carboxyl terminal region of the delta subunit. Control anti-AChR mAbs specific for the alpha or the delta subunits, whose epitopes have known transmembrane topology, uniquely recognized the expected side of the postsynaptic membrane. Residues involved in C delta-mAb binding were identified using single residue substituted peptide analogues of the sequence delta 481-501. All C delta-mAbs recognized epitopes within the same sequence segment, delta 485-493, at the carboxyl terminal of the AChR delta subunit. These results suggest thatthe delta subunit of the AChR might have alternative conformations, leading to exposure of the same sequence region on the extracellular orthe cytoplasmic surface. Several Pro residues are present in this region. The alternative cis or trans conformation of one or more of them might result in different folding patterns of the carboxyl terminal sequence of the delta subunit, as described for a viral protein [Liddington, R. C., Yan, Y., Moulai, J., Sahli, R., Benjamin, T. L., and Harrison, S. C. (1991) Nature 354, 278-284].

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 09:34:07