| pubmed-article:8457543 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C0040549 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C0205217 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C0038477 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C0036451 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C1548700 | lld:lifeskim |
| pubmed-article:8457543 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8457543 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:8457543 | pubmed:dateCreated | 1993-4-23 | lld:pubmed |
| pubmed-article:8457543 | pubmed:abstractText | The venom of the scorpion Androctonus mauretanicus mauretanicus contains a toxin, P05, which is structurally and functionally similar to scorpion leiurotoxin I (87% sequence identity), a blocker of the apamin-sensitive Ca(2+)-activated K+ channels. It is a 31-residue polypeptide cross-linked by three disulfide bridges. A C-terminal carboxyl-amidated analog of P05 (sP05-NH2) was chemically synthesized by the solid-phase technique and fully characterized. Toxicity assays in vivo established that sP05-NH2, like native P05, is a potent and lethal neurotoxic agent in mice (LD50 of 20 ng per mouse). Pharmacological assays in vitro however showed that, unlike P05 which has a binding affinity of 2 x 10(-11) M, sP05-NH2 apparently binds irreversibly to the apamin receptor. Iodination at the C-terminal His gave diiodo-sP05-NH2, which had a binding affinity similar to that of native P05. The disulfide bridge pairings were chemically determined for sP05-NH2 and thereby deduced for P05 and leiurotoxin I: linkages were between Cys3 and Cys21, Cys8 and Cys26, and Cys12 and Cys28. Molecular dynamics refinement of P05 also using data from leiurotoxin I suggests that P05 is mainly composed of a double-stranded, antiparallel beta-sheet (from Leu18 to Val29) linked to an alpha-helix (from Arg6 to Gly16) by two disulfides (Cys8-Cys26 and Cys12-Cys28) and to an extended fragment (from Thr1 to Leu5) by the third disulfide (Cys3-Cys21). In agreement with the model, circular dichroism analysis of sP05-NH2 showed that the toxin structure is highly rigid.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:8457543 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8457543 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457543 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8457543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8457543 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8457543 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8457543 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8457543 | pubmed:author | pubmed-author:RochatHH | lld:pubmed |
| pubmed-article:8457543 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:8457543 | pubmed:author | pubmed-author:Martin-Eaucla... | lld:pubmed |
| pubmed-article:8457543 | pubmed:author | pubmed-author:DarbonHH | lld:pubmed |
| pubmed-article:8457543 | pubmed:author | pubmed-author:MabroukKK | lld:pubmed |
| pubmed-article:8457543 | pubmed:author | pubmed-author:BenslimaneAA | lld:pubmed |
| pubmed-article:8457543 | pubmed:author | pubmed-author:SabatierJ MJM | lld:pubmed |
| pubmed-article:8457543 | pubmed:author | pubmed-author:ZerroukHH | lld:pubmed |
| pubmed-article:8457543 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8457543 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:8457543 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8457543 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8457543 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8457543 | pubmed:pagination | 2763-70 | lld:pubmed |
| pubmed-article:8457543 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8457543 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8457543 | pubmed:articleTitle | P05, a new leiurotoxin I-like scorpion toxin: synthesis and structure-activity relationships of the alpha-amidated analog, a ligand of Ca(2+)-activated K+ channels with increased affinity. | lld:pubmed |
| pubmed-article:8457543 | pubmed:affiliation | Laboratoire de Biochimie, CNRS URA 1455, Faculté de Médecine Nord, Marseille, France. | lld:pubmed |
| pubmed-article:8457543 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8457543 | pubmed:publicationType | Comparative Study | lld:pubmed |
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