The structure of testis angiotensin-converting enzyme (tACE-g13) in complex with the inhibitor RXPA380

Master Thesis

2006

Permanent link to this Item
http://hdl.handle.net/11427/4248
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thesis_sci_2006_chitapi_i.pdf (6.8 MB)
Authors
Chitapi, Itai
Supervisors
Sewell, Bryan Trevor
Sturrock, E D
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University of Cape Town

Department
Department of Molecular and Cell Biology
Faculty
Faculty of Science
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Abstract
Angiotensin-converting enzyme (ACE), a zinc metalloprotease, is a key regulator of the mammalian renin-angiotensin system (RAS) Primarily, ACF is a dipeptidl peptidase which cleaves angiotensin I to produce angiotensin II, a potent vasoconstrictor. By the same enzymatic mechanism, ACE also inactivates the vasodilator bradykinin. The main overall effect of these actions is an increase in blood pressure. Several ACF inhibitors have been developed as drugs for the treatment of myocardial infarction, hypertension, kidney failure and heart failure.
Description

Includes bibliographical references.

Keywords
Structural Biology

Reference:

Chitapi, I. 2006. The structure of testis angiotensin-converting enzyme (tACE-g13) in complex with the inhibitor RXPA380. University of Cape Town.

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