Mechanistic insight into the function of the C-terminal PKD domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: binding of the PKD domain to collagen results in collagen swelling but does not unwind the collagen triple helix.

@article{Wang2010MechanisticII,
  title={Mechanistic insight into the function of the C-terminal PKD domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: binding of the PKD domain to collagen results in collagen swelling but does not unwind the collagen triple helix.},
  author={Yu-Kai Wang and Guo-Yan Zhao and Yang Li and Xiu-lan Chen and Bin-Bin Xie and H Su and Yao-hui Lv and Hongyong He and Hong Liu and Jun Hu and Bai-cheng Zhou and Yu-Zhong Zhang},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 19},
  pages={14285-91}
}
Deseasin MCP-01 is a bacterial collagenolytic serine protease. Its catalytic domain alone can degrade collagen, and its C-terminal PKD domain is a collagen-binding domain (CBD) that can improve the collagenolytic efficiency of the catalytic domain by an unknown mechanism. Here, scanning electron microscopy (SEM), atomic force microscopy (AFM), zeta potential, and circular dichroism spectroscopy were used to clarify the functional mechanism of the PKD domain in MCP-01 collagenolysis. The PKD… CONTINUE READING

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