Probing the Agonist Domain of the Nicotinic Acetylcholine Receptor by Cysteine Scanning Mutagenesis Reveals Residues in Proximity to the α-Bungarotoxin Binding Site-Reference-Cited by-同舟云学术

Probing the Agonist Domain of the Nicotinic Acetylcholine Receptor by Cysteine Scanning Mutagenesis Reveals Residues in Proximity to the α-Bungarotoxin Binding Site

Published:1999-04-01 Issue:16 Volume:38 Page:4912-4921
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Spura Armin¹,Russin Tanya S.¹,Freedman Neal D.¹,Grant Marianne¹,McLaughlin James T.¹,Hawrot Edward¹

Affiliation:

1. Department of Molecular Pharmacology, Physiology and Biotechnology, Division of Biology and Medicine, Brown University, Providence, Rhode Island 02912, 401-863-1283, and Department of Pharmacology, Tufts University, 136 Harrison Street, Boston, Massachusetts 02111

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi982656z

Reference56 articles.

1. The Handedness of the Subunit Arrangement of the Nicotinic Acetylcholine Receptor from Torpedo californica

2. Restoration of 125I-alpha-bungarotoxin binding activity to the alpha subunit of Torpedo acetylcholine receptor isolated by gel electrophoresis in sodium dodecyl sulfate.

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