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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

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Orzáez Calatayud, María del Mar; Lukovic, Dunja; Abad Mazario, Concepción; Pérez Payá, Enrique; Mingarro Muñoz, Ismael

Aquest document és un/a article, creat/da en: 2005

The principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimer- isation motif that mediates transmembrane (TM) helix associa- tion, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Fur- ther, we have used this minimised GpA motif to assess the influ- ence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix-helix association and/or dissociation between TM fragments.

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