skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Dihydropyridine receptor of L-type Ca sup 2+ channels: Identification of binding domains for ( sup 3 H)(+)-PN200-110 and ( sup 3 H)azidopine within the. alpha. 1 subunit

Abstract

To identify the binding domain for dihydropyridine Ca{sup 2{plus}} antagonists, skeletal muscle Ca{sup 2{plus}} channels were photolabeled with ({sup 3}H)({plus})-PN200-110 and ({sup 3}H) azidopine. Regions of {alpha}1 photolabeled by these ligands were then identified by antibody mapping of proteolytic fragments. Approximately 50% of the specific labeling by both ligands was incorporated in domain III. ({sup 3}H)Azidopine labeled peptide Gln-989-Arg-1022, which contains a portion of the connecting loop between transmembrane segments IIIS5 and IIIS6 (IIIS5/S6), and peptide Ala-1023-Lys-1077, which contains IIIS6 itself and some adjacent amino acid residues. In contrast, ({sup 3}H)({plus})-PN200-110 labeling occurred almost exclusively in the fragment containing IIIS6. A second site labeled by both ligands was identified in transmembrane segment S6 of domain IV and adjacent residues. It is proposed, based on physiological studies, that these three peptide segments interact to form a receptor site accessible from the extracellular surface of the Ca{sup 2{plus}} channel.

Authors:
; ;  [1]
  1. (Univ. of Washington, Seattle (United States))
Publication Date:
OSTI Identifier:
5821390
Resource Type:
Journal Article
Resource Relation:
Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States); Journal Volume: 88:23
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; AZIDO COMPOUNDS; RADIORECEPTOR ASSAY; RECEPTORS; MOLECULAR STRUCTURE; ALANINES; LIGANDS; LYSINE; PYRIDINES; TRITIUM COMPOUNDS; AMINO ACIDS; AZINES; CARBOXYLIC ACIDS; HETEROCYCLIC COMPOUNDS; HYDROGEN COMPOUNDS; ISOTOPE APPLICATIONS; MEMBRANE PROTEINS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; PROTEINS; TRACER TECHNIQUES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Striessnig, J., Murphy, B.J., and Catterall, W.A.. Dihydropyridine receptor of L-type Ca sup 2+ channels: Identification of binding domains for ( sup 3 H)(+)-PN200-110 and ( sup 3 H)azidopine within the. alpha. 1 subunit. United States: N. p., 1991. Web. doi:10.1073/pnas.88.23.10769.
Striessnig, J., Murphy, B.J., & Catterall, W.A.. Dihydropyridine receptor of L-type Ca sup 2+ channels: Identification of binding domains for ( sup 3 H)(+)-PN200-110 and ( sup 3 H)azidopine within the. alpha. 1 subunit. United States. doi:10.1073/pnas.88.23.10769.
Striessnig, J., Murphy, B.J., and Catterall, W.A.. Sun . "Dihydropyridine receptor of L-type Ca sup 2+ channels: Identification of binding domains for ( sup 3 H)(+)-PN200-110 and ( sup 3 H)azidopine within the. alpha. 1 subunit". United States. doi:10.1073/pnas.88.23.10769.
@article{osti_5821390,
title = {Dihydropyridine receptor of L-type Ca sup 2+ channels: Identification of binding domains for ( sup 3 H)(+)-PN200-110 and ( sup 3 H)azidopine within the. alpha. 1 subunit},
author = {Striessnig, J. and Murphy, B.J. and Catterall, W.A.},
abstractNote = {To identify the binding domain for dihydropyridine Ca{sup 2{plus}} antagonists, skeletal muscle Ca{sup 2{plus}} channels were photolabeled with ({sup 3}H)({plus})-PN200-110 and ({sup 3}H) azidopine. Regions of {alpha}1 photolabeled by these ligands were then identified by antibody mapping of proteolytic fragments. Approximately 50% of the specific labeling by both ligands was incorporated in domain III. ({sup 3}H)Azidopine labeled peptide Gln-989-Arg-1022, which contains a portion of the connecting loop between transmembrane segments IIIS5 and IIIS6 (IIIS5/S6), and peptide Ala-1023-Lys-1077, which contains IIIS6 itself and some adjacent amino acid residues. In contrast, ({sup 3}H)({plus})-PN200-110 labeling occurred almost exclusively in the fragment containing IIIS6. A second site labeled by both ligands was identified in transmembrane segment S6 of domain IV and adjacent residues. It is proposed, based on physiological studies, that these three peptide segments interact to form a receptor site accessible from the extracellular surface of the Ca{sup 2{plus}} channel.},
doi = {10.1073/pnas.88.23.10769},
journal = {Proceedings of the National Academy of Sciences of the United States of America; (United States)},
number = ,
volume = 88:23,
place = {United States},
year = {Sun Dec 01 00:00:00 EST 1991},
month = {Sun Dec 01 00:00:00 EST 1991}
}