The 2.1-A crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability.

@article{Takehara2009The2C,
  title={The 2.1-A crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability.},
  author={Sayaka Takehara and Maki Onda and Juan Zhang and Mika Nishiyama and Xiaojing Yang and Bunzo Mikami and David A. Lomas},
  journal={Journal of molecular biology},
  year={2009},
  volume={388 1},
  pages={
          11-20
        }
}
Neuroserpin is a selective inhibitor of tissue-type plasminogen activator (tPA) that plays an important role in neuronal plasticity, memory, and learning. We report here the crystal structure of native human neuroserpin at 2.1 A resolution. The structure has a helical reactive center loop and an omega loop between strands 1B and 2B. The omega loop contributes to the inhibition of tPA, as deletion of this motif reduced the association rate constant with tPA by threefold but had no effect on the… CONTINUE READING

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