Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability.

@article{Flaugh2005InterdomainSI,
  title={Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability.},
  author={Shannon L Flaugh and Melissa Kosinski-Collins and Jonathan Alan King},
  journal={Protein science : a publication of the Protein Society},
  year={2005},
  volume={14 8},
  pages={2030-43}
}
Human gammaD crystallin (HgammaD-Crys) is a two domain, beta-sheet eye lens protein that must remain soluble throughout life for lens transparency. Single amino acid substitutions of HgammaD-Crys are associated with juvenile-onset cataracts. Features of the interface between the two domains conserved among gamma-crystallins are a central six-residue hydrophobic cluster, and two pairs of interacting residues flanking the cluster. In HgammaD-Crys these pairs are Gln54/Gln143 and Arg79/Met147. We… CONTINUE READING

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