Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution.

@article{Li2006AnnularAA,
  title={Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution.},
  author={Sheng-jian Li and Xin-guo Hong and Yuan-Yuan Shi and Hui Li and Chih-Chen Wang},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 10},
  pages={
          6581-8
        }
}
We presented for the first time a small angle x-ray scattering study of intact protein-disulfide isomerase (PDI) in solution. The restored model revealed that PDI is a short and roughly elliptical cylinder with a molecular mass of 69 kDa and dimensions of 105 x 65 x 40 A, and the four thioredoxin-fold domains in the order a-b-b'-a' are arranged in an annular fashion. Atomic force microscope imaging also supported the finding that PDI appears as an approximately flat elliptical cylinder. A PDI… CONTINUE READING

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