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

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 Perfil
This document is a artículoDate2005

Este documento está disponible también en : http://hdl.handle.net/10550/65663
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.

    Orzáez Calatayud, María del Mar Lukovic, Dunja Abad Mazario, Concepción Pérez Payá, Enrique Mingarro Muñoz, Ismael 2005 Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif Febs Letters 579 7 1633 1638
https://doi.org/10.1016/j.febslet.2005.01.078

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