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Titolo:
AMINO-ACIDS WITHIN RESIDUE-181-200 OF THE NICOTINIC ACETYLCHOLINE-RECEPTOR ALPHA-1 SUBUNIT INVOLVED IN NICOTINE BINDING
Autore:
LENTZ TL; CHATURVEDI V; CONTIFINE BM;
Indirizzi:
YALE UNIV,SCH MED,DEPT CELL BIOL,333 CEDAR ST,POB 208002 NEW HAVEN CT06520 UNIV MINNESOTA,COLL BIOL SCI,DEPT BIOCHEM ST PAUL MN 55108
Titolo Testata:
Biochemical pharmacology
fascicolo: 3, volume: 55, anno: 1998,
pagine: 341 - 347
SICI:
0006-2952(1998)55:3<341:AWROTN>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
BUNGAROTOXIN-BINDING; CONSERVED TYROSINES; SITE DISULFIDE; DELTA-SUBUNIT; TORPEDO; IDENTIFICATION; ALPHA-1-SUBUNIT; SUBSTITUTIONS; MUTATIONS; SEQUENCE;
Keywords:
ACETYLCHOLINE RECEPTOR; AMINO ACIDS; FUSION PROTEINS; NICOTINE; STRUCTURE-FUNCTION RELATIONSHIPS; SYNTHETIC PEPTIDES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
T.L. Lentz et al., "AMINO-ACIDS WITHIN RESIDUE-181-200 OF THE NICOTINIC ACETYLCHOLINE-RECEPTOR ALPHA-1 SUBUNIT INVOLVED IN NICOTINE BINDING", Biochemical pharmacology, 55(3), 1998, pp. 341-347

Abstract

Structural determinants of L-[H-3]nicotine binding to the sequence flanking Cys 192 and Cys 193 of the Torpedo acetylcholine receptor alpha1 subunit were investigated using synthetic peptides (residues 181-200) and fusion proteins (residues 166-211). Nicotine binding at a single concentration (30 nM) was compared with 71 peptides and fusion proteins in which individual amino acids at positions 181-200 were substituted. Substitution of Lys 185, Tyr 190, Cys 192, Cys 193, Thr 196, and Tyr 198 resulted in the greatest reduction in nicotine binding. Equilibrium binding of [H-3]nicotine to peptide 181-200 revealed a binding component with an apparent K-D of 1.2 mu M. Substitution of Lys 185 (with Glu), His 186, Tyr 190, Cys 192, Cys 193, and Tyr 198 resulted in asignificant reduction in affinity. Affinity was not affected significantly by substitution of Arg 182, Lys 185 (with Gly or Arg), Val 188, Tyr 189, Pro 194, Asp 195, Thr 196, and Asp 200. It is concluded that Lys 185, His 186, Tyr 190, Cys 192, Cys 193, and Tyr 198 play the greatest role in nicotine binding to residues 181-200 of the alpha 1 subunit. Previous studies have implicated Tyr 190, Cys 192, Cys 193, and Tyr 198 in agonist binding to the acetylcholine receptor. These results confirm a role for these residues and also demonstrate a function for Lys 185 and His 186 in nicotine binding. (C) 1998 Elsevier Science Inc.

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Documento generato il 01/10/20 alle ore 07:36:09