| pubmed-article:10493862 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10493862 | lifeskim:mentions | umls-concept:C0037492 | lld:lifeskim |
| pubmed-article:10493862 | lifeskim:mentions | umls-concept:C0040549 | lld:lifeskim |
| pubmed-article:10493862 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:10493862 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:10493862 | lifeskim:mentions | umls-concept:C0678595 | lld:lifeskim |
| pubmed-article:10493862 | lifeskim:mentions | umls-concept:C0036451 | lld:lifeskim |
| pubmed-article:10493862 | lifeskim:mentions | umls-concept:C1504308 | lld:lifeskim |
| pubmed-article:10493862 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10493862 | pubmed:dateCreated | 1999-10-20 | lld:pubmed |
| pubmed-article:10493862 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493862 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493862 | pubmed:abstractText | The crystal structures of two group III alpha-like toxins from the scorpion Buthus martensii Karsch, BmK M1 and BmK M4, were determined at 1.7 A and 1.3 A resolution and refined to R factors of 0.169 and 0.166, respectively. The first high-resolution structures of the alpha-like scorpion toxin show some striking features compared with structures of the "classical" alpha-toxin. Firstly, a non-proline cis peptide bond between residues 9 and 10 unusually occurs in the five-member reverse turn 8-12. Secondly, the cis peptide 9-10 mediates the spatial relationship between the turn 8-12 and the C-terminal stretch 58-64 through a pair of main-chain hydrogen bonds between residues 10 and 64 to form a unique tertiary arrangement which features the special orientation of the terminal residues 62-64. Finally, in consequence of the peculiar orientation of the C-terminal residues, the functional groups of Arg58, which are crucial for the toxin-receptor interaction, are exposed and accessible in BmK M1 and M4 rather than buried as in the classical alpha-toxins. Sequence alignment and characteristics analysis suggested that the above structural features observed in BmK M1 and M4 occur in all group III alpha-like toxins. Recently, some group III alpha-like toxins were demonstrated to occupy a receptor site different from the classical alpha-toxin. Therefore, the distinct structural features of BmK M1 and M4 presented here may provide the structural basis for the newly recognized toxin-receptor binding site selectivity. Besides, the non-proline cis peptide bonds found in these two structures play a role in the formation of the structural characteristics and in keeping accurate positions of the functionally crucial residues. This manifested a way to achieve high levels of molecular specificity and atomic precision through the strained backbone geometry. | lld:pubmed |
| pubmed-article:10493862 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10493862 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493862 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10493862 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493862 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493862 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493862 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493862 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10493862 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10493862 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10493862 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:10493862 | pubmed:author | pubmed-author:WangD CDC | lld:pubmed |
| pubmed-article:10493862 | pubmed:author | pubmed-author:YungK HKH | lld:pubmed |
| pubmed-article:10493862 | pubmed:author | pubmed-author:WangMM | lld:pubmed |
| pubmed-article:10493862 | pubmed:author | pubmed-author:LiuX QXQ | lld:pubmed |
| pubmed-article:10493862 | pubmed:author | pubmed-author:MAH THT | lld:pubmed |
| pubmed-article:10493862 | pubmed:author | pubmed-author:HeX LXL | lld:pubmed |
| pubmed-article:10493862 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10493862 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10493862 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:10493862 | pubmed:volume | 292 | lld:pubmed |
| pubmed-article:10493862 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10493862 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10493862 | pubmed:pagination | 125-35 | lld:pubmed |
| pubmed-article:10493862 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10493862 | pubmed:meshHeading | pubmed-meshheading:10493862... | lld:pubmed |
| pubmed-article:10493862 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10493862 | pubmed:articleTitle | Crystal structures of two alpha-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel. | lld:pubmed |
| pubmed-article:10493862 | pubmed:affiliation | Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, P.R. China. | lld:pubmed |
| pubmed-article:10493862 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10493862 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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