N-Terminal domain of Bombyx mori fibroin mediates the assembly of silk in response to pH decrease.

@article{He2012NTerminalDO,
  title={N-Terminal domain of Bombyx mori fibroin mediates the assembly of silk in response to pH decrease.},
  author={Y He and Nan-nan Zhang and Wei-Fang Li and Ning Jia and Bao-yu Chen and Kang Zhou and Jiahai Zhang and Y Chen and Cong-Zhao Zhou},
  journal={Journal of molecular biology},
  year={2012},
  volume={418 3-4},
  pages={197-207}
}
Fibroins serve as the major building blocks of silk fiber. As the major component of fibroin, the fibroin heavy chain is a considerably large protein comprising N-terminal and C-terminal hydrophilic domains and 12 highly repetitive Gly-Ala-rich regions flanked by internal hydrophilic blocks. Here, we show the crystal structure of the fibroin N-terminal domain (FibNT) at pH 4.7, revealing a remarkable double-layered anti-parallel β-sheet with each layer comprising two FibNT molecules entangled… CONTINUE READING
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