| pubmed-article:2557622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2557622 | lifeskim:mentions | umls-concept:C0002812 | lld:lifeskim |
| pubmed-article:2557622 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
| pubmed-article:2557622 | lifeskim:mentions | umls-concept:C0037492 | lld:lifeskim |
| pubmed-article:2557622 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:2557622 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:2557622 | lifeskim:mentions | umls-concept:C1283195 | lld:lifeskim |
| pubmed-article:2557622 | lifeskim:mentions | umls-concept:C0002309 | lld:lifeskim |
| pubmed-article:2557622 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:2557622 | pubmed:dateCreated | 1990-2-1 | lld:pubmed |
| pubmed-article:2557622 | 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. | lld:pubmed |
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| pubmed-article:2557622 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2557622 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2557622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2557622 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2557622 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2557622 | pubmed:author | pubmed-author:CatterallW... | lld:pubmed |
| pubmed-article:2557622 | pubmed:author | pubmed-author:ThomsenW JWJ | lld:pubmed |
| pubmed-article:2557622 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2557622 | pubmed:volume | 86 | lld:pubmed |
| pubmed-article:2557622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2557622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2557622 | pubmed:pagination | 10161-5 | lld:pubmed |
| pubmed-article:2557622 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2557622 | pubmed:meshHeading | pubmed-meshheading:2557622-... | lld:pubmed |
| pubmed-article:2557622 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2557622 | pubmed:articleTitle | Localization of the receptor site for alpha-scorpion toxins by antibody mapping: implications for sodium channel topology. | lld:pubmed |
| pubmed-article:2557622 | pubmed:affiliation | Department of Pharmacology, School of Medicine, University of Washington, Seattle 98195. | lld:pubmed |
| pubmed-article:2557622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2557622 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2557622 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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