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

Research output: Contribution to journalArticlepeer-review

  • M. Badasso
  • C. Frazao
  • B. L. Sibanda
  • V. Dhanaraj
  • C. Dealwis
  • J. B. Cooper
  • Professor Steve 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
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
Issue number2
Publication statusPublished - 1 Jan 1992

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