The X-ray crystal structure of human aminopeptidase N reveals a novel dimer and the basis for peptide processing.

@article{Wong2012TheXC,
  title={The X-ray crystal structure of human aminopeptidase N reveals a novel dimer and the basis for peptide processing.},
  author={Alan H. M. Wong and Dongxia Zhou and James M. Rini},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 44},
  pages={36804-13}
}
Human aminopeptidase N (hAPN/hCD13) is a dimeric membrane protein and a member of the M1 family of zinc metallopeptidases. Within the rennin-angiotensin system, its enzymatic activity is responsible for processing peptide hormones angiotensin III and IV. In addition, hAPN is also involved in cell adhesion, endocytosis, and signal transduction and it is an important target for cancer therapy. Reported here are the high resolution x-ray crystal structures of the dimeric ectodomain of hAPN and its… CONTINUE READING
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