Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan.

@article{Scott2004CrystalSO,
  title={Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan.},
  author={Paul G. Scott and Paul A. McEwan and Carole M. Dodd and Ernst M Bergmann and Paul N. Bishop and Jordi Bella},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 44},
  pages={15633-8}
}
Decorin is a ubiquitous extracellular matrix proteoglycan with a variety of important biological functions that are mediated by its interactions with extracellular matrix proteins, cytokines, and cell surface receptors. Decorin is the prototype of the family of small leucine-rich repeat proteoglycans and proteins (SLRPs), characterized by a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions. We report here the crystal structure of the dimeric protein core… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 61 extracted citations

References

Publications referenced by this paper.

The PYMOL Molecular Graphics System (DeLano

  • W. L. DeLano
  • 2002

Similar Papers

Loading similar papers…