Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design.

@article{Corradi2006CrystalSO,
  title={Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design.},
  author={Hazel R. Corradi and Sylva L. U. Schwager and Aloysius T Nchinda and Edward D. Sturrock and Keshab R. Acharya},
  journal={Journal of molecular biology},
  year={2006},
  volume={357 3},
  pages={964-74}
}
Human somatic angiotensin I-converting enzyme (sACE) is a key regulator of blood pressure and an important drug target for combating cardiovascular and renal disease. sACE comprises two homologous metallopeptidase domains, N and C, joined by an inter-domain linker. Both domains are capable of cleaving the two hemoregulatory peptides angiotensin I and bradykinin, but differ in their affinities for a range of other substrates and inhibitors. Previously we determined the structure of testis ACE (C… CONTINUE READING

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