Three-dimensional structure of α-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6.

@article{Baranova2011ThreedimensionalSO,
  title={Three-dimensional structure of α-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6.},
  author={Ekaterina Vitalievna Baranova and Stephen D Weeks and Steven Beelen and Olesya V. Bukach and Nikolai B Gusev and Sergei V. Strelkov},
  journal={Journal of molecular biology},
  year={2011},
  volume={411 1},
  pages={110-22}
}
Small heat shock proteins (sHSPs) are a family of evolutionary conserved ATP-independent chaperones. These proteins share a common architecture defined by a signature α-crystallin domain (ACD) flanked by highly variable N- and C-terminal extensions. The ACD, which has an immunoglobulin-like fold, plays an important role in sHSP assembly. This domain mediates dimer formation of individual protomers, which then may assemble into larger oligomers. In vertebrate sHSPs, the dimer interface is formed… CONTINUE READING

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