Crystallization and preliminary X-ray analysis of complexes of peptide inhibitors with human recombinant and mouse submandibular renins

M. Badasso, C. Frazao, B. L. Sibanda, V. Dhanaraj, C. Dealwis, J. B. Cooper, S. P. Wood, T. L. Blundell, K. Murakami, H. Miyazaki, P. M. Hobart, K. F. Geoghegan, M. J. Ammirati, A. J. Lanzetti, D. E. Danley, B. A. O'Connor, D. J. Hoover, J. Sueiras-diaz, D. M. Jones, M. Szelke

Research output: Contribution to journalArticlepeer-review

Abstract

Inhibitor-complexed crystals of mouse and human renins suitable for X-ray analysis have been prepared. The mouse renin is complexed with a non-hydrolysable decapeptide analogue of rat angiotensinogen containing a hydroxyethylene isostere in place of the scissile bond. The crystals are monoclinic, space group P2(1) with cell dimensions a = 78.3 Å, b = 117.8 Å, c = 85.9 A, β = 101.18 degrees containing four molecules per asymmetric unit. The human renin is fully glycosylated and complexed with a tetrapeptide containing norstatine. The complex crystallises in the cubic space group P2(1)3 with a = 143.1 Å and has two molecules in the asymmetric unit. The rotation function of the mouse renin complex indicates pseudo 222 symmetry while that of human renin indicates a pseudo 2-fold axis. Full structural analyses of the two complexes are underway.
Original languageEnglish
Pages (from-to)447-453
JournalJournal of Molecular Biology
Volume223
Issue number2
DOIs
Publication statusPublished - 1 Jan 1992

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