Intermonomer hydrogen bonds enhance GxxxG-driven dimerization of the BNIP3 transmembrane domain: roles for sequence context in helix-helix association in membranes.

@article{Lawrie2010IntermonomerHB,
  title={Intermonomer hydrogen bonds enhance GxxxG-driven dimerization of the BNIP3 transmembrane domain: roles for sequence context in helix-helix association in membranes.},
  author={Charles M Lawrie and Endah S Sulistijo and Kevin Mackenzie},
  journal={Journal of molecular biology},
  year={2010},
  volume={396 4},
  pages={924-36}
}
We determined the sequence dependence of human BNIP3 transmembrane domain dimerization using the biological assay TOXCAT. Mutants in which intermonomer hydrogen bonds between Ser172 and His173 are abolished show moderate interaction, indicating that side-chain hydrogen bonds contribute to dimer stability but are not essential to dimerization. Mutants in which a GxxxG motif composed of Gly180 and Gly184 has been abolished show little or no interaction, demonstrating the critical nature of the… CONTINUE READING
8 Citations
37 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 37 references

Similar Papers

Loading similar papers…