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Three-dimensional structure, specificity and catalytic mechanism of renin

Nature volume 304, pages 273–275 (1983)Cite this article

Abstract

Renin is an aspartyl proteinase that catalyses the first, and rate-limiting, step in the conversion of angiotensinogen to the hormone angiotensin II1. The catalysis is highly specific, and plays an important physiological part in the regulation of blood pressure2. For this reason inhibitors of renin are of potential value in the treatment of certain forms of hypertension. Although progress has been made in the design of inhibitors for clinical use by modification of angiotensinogen sequences3, and as pepstatin analogues4 or with reduced peptide bonds5, we have now provided the basis for a more rational approach by the use of interactive computer graphics techniques to build a three-dimensional model of renin. The model is based on the three-dimensional structure of endothia pepsin and the primary structure of mouse renin6,7, which is very similar to that of the human enzyme8. We show that renin may have a three-dimensional structure similar to that of other aspartyl proteinases9–11.

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Authors and Affiliations

  1. Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, University of London, Malet Street, London, WC1E 7HX, UK

    Tom Blundell, Bancinyane Lynn Sibanda & Laurence Pearl

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  1. Tom Blundell
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  2. Bancinyane Lynn Sibanda
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  3. Laurence Pearl
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Blundell, T., Sibanda, B. & Pearl, L. Three-dimensional structure, specificity and catalytic mechanism of renin. Nature 304, 273–275 (1983). https://doi.org/10.1038/304273a0

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