Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues.

@article{Zhang2009TransmembraneHA,
  title={Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues.},
  author={Jinming Zhang and Themis Lazaridis},
  journal={Biophysical journal},
  year={2009},
  volume={96 11},
  pages={4418-27}
}
The GxxxG sequence motif mediates the association of transmembrane (TM) helices by providing a site of close contact between them. However, it is not sufficient for strong association. For example, both bacteriophage M13 major coat protein (MCP) and human erythrocyte protein glycophorin A (GpA) contain a GxxxG motif in their TM domains and form a homodimer, but the association affinity of MCP, measured by the ToxCAT in vivo assay, is dramatically weaker than that of GpA. Even when all… CONTINUE READING

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