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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1998-6-4
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pubmed:abstractText |
The glycophorin A transmembrane segment homo-dimerizes to a right-handed pair of alpha-helices. Here, we identified the amino acid motif mediating this interaction within a natural membrane environment. Critical residues were grafted onto two different hydrophobic host sequences in a stepwise manner and self-assembly of the hybrid sequences was determined with the ToxR transcription activator system. Our results show that the motif LIxxGxxxGxxxT elicits a level of self-association equivalent to that of the original glycophorin A transmembrane segment. This motif is very similar to the one previously established in detergent solution. Interestingly, the central GxxxG motif by itself already induced strong self-assembly of host sequences and the three-residue spacing between both glycines proved to be optimal for the interaction. The GxxxG element thus appears to be the most crucial part of the interaction motif.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-1329208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-1560773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-3278900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-3323813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-7592855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-7656033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-7664730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-7666434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-7775472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-7984776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-8663163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-8918935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568912-9266169
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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 |
Apr
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1052-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9568912-Bacterial Proteins,
pubmed-meshheading:9568912-Cell Division,
pubmed-meshheading:9568912-Cell Line,
pubmed-meshheading:9568912-DNA-Binding Proteins,
pubmed-meshheading:9568912-Dimerization,
pubmed-meshheading:9568912-Glycine,
pubmed-meshheading:9568912-Glycophorin,
pubmed-meshheading:9568912-Maltose,
pubmed-meshheading:9568912-Membrane Proteins,
pubmed-meshheading:9568912-Promoter Regions, Genetic,
pubmed-meshheading:9568912-Protein Conformation,
pubmed-meshheading:9568912-Protein Engineering,
pubmed-meshheading:9568912-Protein Structure, Secondary,
pubmed-meshheading:9568912-Recombinant Fusion Proteins,
pubmed-meshheading:9568912-Transcription Factors,
pubmed-meshheading:9568912-Transcriptional Activation
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pubmed:year |
1998
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pubmed:articleTitle |
The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues.
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pubmed:affiliation |
Universität Heidelberg, Neurobiologie Department, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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