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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design
Journal of Molecular Biology, Volume 357, No. 3, Year 2006
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Description
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 domain); here we present the crystal structure of the N domain of sACE (both in the presence and absence of the antihypertensive drug lisinopril) in order to aid the understanding of how these two domains differ in specificity and function. In addition, the structure of most of the inter-domain linker allows us to propose relative domain positions for sACE that may contribute to the domain cooperativity. The structure now provides a platform for the design of "domain-specific" second-generation ACE inhibitors. © 2006 Elsevier Ltd. All rights reserved.
Authors & Co-Authors
Corradi, Hazel Ruth
United Kingdom, Bath
University of Bath
Schwager, Sylva L.U.
South Africa, Cape Town
University of Cape Town
Nchinda, Aloysius T.
South Africa, Cape Town
University of Cape Town
Sturrock, Edward D.
South Africa, Cape Town
University of Cape Town
Ravi Acharya, K.
United Kingdom, Bath
University of Bath
Statistics
Citations: 140
Authors: 5
Affiliations: 2
Identifiers
Doi:
10.1016/j.jmb.2006.01.048
ISSN:
00222836
Research Areas
Noncommunicable Diseases