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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
1990-2-1
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pubmed:abstractText |
Site-directed and monoclonal antibodies recognizing different extracellular regions of the RII sodium channel alpha subunit have been used to determine the sequences that comprise the receptor for alpha-scorpion toxins by evaluating the effect of antibody on voltage-dependent binding of radio-labeled toxin isolated from Leiurus quinquestriatus to both reconstituted rat brain sodium channel and rat brain synaptosomes. Of six antibodies tested, two recognizing amino acid residues 355-371 and 382-400 located on an extracellular loop between transmembrane segments S5 and S6 of domain I and one recognizing residues 1686-1703 of a similar loop of domain IV inhibit binding by 30-55%. Inhibition is concentration-(EC50 = 0.4-2 microM) and time- (t1/2 = 40-80 min) dependent. Five different monoclonal antibodies recognizing the same extracellular loop in domain I inhibit binding completely with similar EC50 values as observed for site-directed antibodies. Kinetic studies of the antibody effect are consistent with a slowly reversible competition for the toxin receptor site. Our results suggest that the extracellular loops between segments S5 and S6 of domains I and IV comprise at least part of the alpha-scorpion toxin receptor site and support the membrane topology models in which domains I and IV are adjacent in the tertiary structure of the channel protein and six transmembrane sequences are contained in each of the four homologous domains.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2413014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2415395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2417247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2427018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2429308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2432607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2433986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2436544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2446328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2447073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2447092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2458625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2459775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2543931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2554301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2847174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2848108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-2848576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-3174645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-3754035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-479827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-6098308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-6319405,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-6319406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-656383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-6928649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2557622-72754
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10161-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2557622-Animals,
pubmed-meshheading:2557622-Antibodies, Monoclonal,
pubmed-meshheading:2557622-Antigen-Antibody Complex,
pubmed-meshheading:2557622-Brain,
pubmed-meshheading:2557622-Kinetics,
pubmed-meshheading:2557622-Models, Structural,
pubmed-meshheading:2557622-Rats,
pubmed-meshheading:2557622-Receptors, Cholinergic,
pubmed-meshheading:2557622-Scorpion Venoms,
pubmed-meshheading:2557622-Sodium Channels,
pubmed-meshheading:2557622-Synaptosomes
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pubmed:year |
1989
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pubmed:articleTitle |
Localization of the receptor site for alpha-scorpion toxins by antibody mapping: implications for sodium channel topology.
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pubmed:affiliation |
Department of Pharmacology, School of Medicine, University of Washington, Seattle 98195.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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