| pubmed-article:3607056 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C0012550 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C0004927 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C0441587 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:3607056 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:3607056 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3607056 | pubmed:dateCreated | 1987-9-21 | lld:pubmed |
| pubmed-article:3607056 | pubmed:abstractText | The insertion of the A domain of diphtheria toxin into model membranes has been shown to be both pH- and temperature-dependent (Hu and Holmes (1984) J. Biol. Chem. 259, 12226-12233). In this report, the insertion behavior of two mutant proteins of diphtheria toxin, CRM197 and CRM9, was studied and compared to that of wild-type toxin. Results indicated that both CRM197 and CRM9 resembled toxin with respect to the pH-dependence of binding to negatively-charged liposomes at room temperature. However, CRM197 differed from toxin with respect to both the pH- and temperature-dependence of fragment A insertion; fragment A197 inserts more readily into the bilayer at 0 degrees C and low pH or at neutral pH and room temperature than does wild type fragment A under these same conditions. This result indicates that the single amino acid substitution in the A domain of CRM197 facilitates entry of fragment A197 into the membrane, suggesting that CRM197 may be conformationally distinct from native toxin. In fact, the fluorescence spectra of CRM197 and wild-type toxin as well as their respective tryptic peptide patterns indicate that, at pH 7, CRM197 more closely resembles the acid form of wild-type toxin than the native form of toxin. These data suggest that CRM197 may be naturally in a more 'insertion-competent' conformation. In contrast, the mutation in the B domain of CRM9 which results in a 1000-fold decrease in binding affinity for plasma membrane receptors apparently does not cause a change in either the insertion of fragment A9 or the lipid-binding properties of CRM9 relative to toxin. | lld:pubmed |
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| pubmed-article:3607056 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3607056 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3607056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3607056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3607056 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3607056 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:3607056 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:3607056 | pubmed:author | pubmed-author:HolmesR KRK | lld:pubmed |
| pubmed-article:3607056 | pubmed:author | pubmed-author:HuV WVW | lld:pubmed |
| pubmed-article:3607056 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3607056 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:3607056 | pubmed:volume | 902 | lld:pubmed |
| pubmed-article:3607056 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3607056 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3607056 | pubmed:pagination | 24-30 | lld:pubmed |
| pubmed-article:3607056 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:3607056 | pubmed:meshHeading | pubmed-meshheading:3607056-... | lld:pubmed |
| pubmed-article:3607056 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3607056 | pubmed:articleTitle | Single mutation in the A domain of diphtheria toxin results in a protein with altered membrane insertion behavior. | lld:pubmed |
| pubmed-article:3607056 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3607056 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:3607056 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3607056 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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