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Titolo:
NEGATIVELY CHARGED AMINO-ACID-RESIDUES IN THE NICOTINIC RECEPTOR DELTA-SUBUNIT THAT CONTRIBUTE TO THE BINDING OF ACETYLCHOLINE
Autore:
CZAJKOWSKI C; KAUFMANN C; KARLIN A;
Indirizzi:
COLUMBIA UNIV COLL PHYS & SURG,CTR MOLEC RECOGNIT NEW YORK NY 10032 COLUMBIA UNIV COLL PHYS & SURG,DEPT BIOCHEM & MOLEC BIOPHYS NEW YORK NY 10032 COLUMBIA UNIV COLL PHYS & SURG,DEPT PHYSIOL & CELLULAR BIOPHYS NEW YORK NY 10032 COLUMBIA UNIV COLL PHYS & SURG,DEPT NEUROL NEW YORK NY 10032
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 13, volume: 90, anno: 1993,
pagine: 6285 - 6289
SICI:
0027-8424(1993)90:13<6285:NCAITN>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-DIRECTED MUTAGENESIS; TORPEDO-CALIFORNICA; ALPHA-SUBUNIT; GAMMA-SUBUNIT; NUCLEOTIDE-SEQUENCE; XENOPUS OOCYTES; LIGAND-BINDING; BETA-SUBUNIT; EXPRESSION; DISULFIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
C. Czajkowski et al., "NEGATIVELY CHARGED AMINO-ACID-RESIDUES IN THE NICOTINIC RECEPTOR DELTA-SUBUNIT THAT CONTRIBUTE TO THE BINDING OF ACETYLCHOLINE", Proceedings of the National Academy of Sciences of the United Statesof America, 90(13), 1993, pp. 6285-6289

Abstract

In nicotinic receptors, the binding sites for acetylcholine are likely to contain negatively charged amino acid side chains that interact with the positively charged quaternary ammonium group of acetylcholine and of other potent agonists. We previously found that a 61-residue segment of the delta subunit contains aspartate or glutamate residues within 1 nm of cysteines in the acetylcholine binding site on the alpha subunit. We have now mutated, one at a time, the 12 aspartates and glutamates in this segment of the mouse muscle delta subunit and have expressed the mutant receptors in Xenopus oocytes. Both the concentrationof acetylcholine eliciting half-maximal current (K(app)) and the K(i)for the inhibition by acetylcholine of alpha-bungarotoxin binding were increased 100-fold by the mutation of deltaAsp180 to Asn and 10-foldby the mutation of deltaGlu189 to Gln. These two residues, and their homologs in the gamma and epsilon subunits, are likely to contribute to the acetylcholine binding sites.

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Documento generato il 12/07/20 alle ore 05:37:31