| pubmed-article:9568912 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C0017955 | lld:lifeskim |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C0017890 | lld:lifeskim |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9568912 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:9568912 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9568912 | pubmed:dateCreated | 1998-6-4 | lld:pubmed |
| pubmed-article:9568912 | 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. | lld:pubmed |
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| pubmed-article:9568912 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9568912 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9568912 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9568912 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9568912 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:9568912 | pubmed:author | pubmed-author:LangoschDD | lld:pubmed |
| pubmed-article:9568912 | pubmed:author | pubmed-author:BrosioJJ | lld:pubmed |
| pubmed-article:9568912 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9568912 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:9568912 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9568912 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9568912 | pubmed:pagination | 1052-6 | lld:pubmed |
| pubmed-article:9568912 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9568912 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9568912 | pubmed:articleTitle | The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues. | lld:pubmed |
| pubmed-article:9568912 | pubmed:affiliation | Universität Heidelberg, Neurobiologie Department, Germany. | lld:pubmed |
| pubmed-article:9568912 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9568912 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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