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• W2163250635 abstract "Both experimental and statistical searches for specific motifs that mediate transmembrane helix–helix interactions showed that two glycine residues separated by three intervening residues (GxxxG) provide a framework for specific interactions. Further work suggested that other motifs of small residues can mediate the interaction of transmembrane domains, so that the AxxxA-motif could also drive strong interactions of α-helices in soluble proteins. Thus, all these data indicate that a motif of two small residues in a distance of four might be enough to provide a framework for transmembrane helix–helix interaction. To test whether GxxxG is equivalent to (small)xxx(small), we investigated the effect of a substitution of either of the two Gly residues in the glycophorin A GxxxG-motif by Ala or Ser using the recently developed GALLEX system. The results of this mutational study demonstrate that, while a replacement of either of the two Gly by Ala strongly disrupts GpA homo-dimerization, the mutation to Ser partly stabilizes a dimeric structure. We suggest that the Ser residue can form a hydrogen bond with a backbone carbonyl group of the adjacent helix stabilizing a preformed homo-dimer. While (small)xxx(small) serves as a useful clue, the context of adjacent side-chains is essential for stable helix interaction, so each case must be tested." @default.
• W2163250635 created "2016-06-24" @default.
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• W2163250635 date "2004-10-01" @default.
• W2163250635 modified "2023-10-16" @default.
• W2163250635 title "Motifs of Two Small Residues can Assist but are not Sufficient to Mediate Transmembrane Helix Interactions" @default.
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• W2163250635 doi "https://doi.org/10.1016/j.jmb.2004.08.083" @default.
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