Crystal structure of human profilaggrin S100 domain and identification of target proteins annexin II, stratifin and hsp27

@inproceedings{Bunick2015CrystalSO,
  title={Crystal structure of human profilaggrin S100 domain and identification of target proteins annexin II, stratifin and hsp27},
  author={Christopher G Bunick and Richard B. Presland and Owen T. Lawrence and David J Pearton and Leonard M. Milstone and Thomas A Steitz},
  booktitle={The Journal of investigative dermatology},
  year={2015}
}
The fused-type S100 protein profilaggrin and its proteolytic products including filaggrin are important in the formation of a normal epidermal barrier; however, the specific function of the S100 calcium-binding domain in profilaggrin biology is poorly understood. To explore its molecular function, we determined a 2.2 Å-resolution crystal structure of the N-terminal fused-type S100 domain of human profilaggrin with bound calcium ions. The profilaggrin S100 domain formed a stable dimer, which… CONTINUE READING

References

Publications referenced by this paper.
SHOWING 1-10 OF 15 REFERENCES

The biochemistry and regulation of S100A10: a multifunctional plasminogen receptor involved in oncogenesis

Pa Madureira, O Connell, Pa Surette, Ap
  • J Biomed Biotechnol
  • 2012