Crystal Structure of the N Domain of Human Somatic Angiotensin I-Converting Enzyme Provides a Structural Basis for Domain-Specific Inhibitor Design.
作者： Hazel R. Corradi , Sylva L.U. Schwager , Aloysius T. Nchinda , Edward D. Sturrock , K. Ravi Acharya
DOI: 10.1016/J.JMB.2006.01.048
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摘要: Human somatic angiotensin I-converting enzyme (sACE) is a key regulator of blood pressure and an important drug target for combating cardiovascular renal disease. sACE comprises two homologous metallopeptidase domains, N C, joined by inter-domain linker. Both domains are capable cleaving the hemoregulatory peptides I bradykinin, but differ in their affinities range other substrates inhibitors. Previously we determined structure testis ACE (C domain); here present crystal domain (both presence absence antihypertensive lisinopril) order to aid understanding how these specificity function. In addition, most linker allows us propose relative positions that may contribute cooperativity. The now provides platform design "domain-specific" second-generation
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