CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF COMPLEXES OF PEPTIDE INHIBITORS WITH HUMAN RECOMBINANT AND MOUSE SUBMANDIBULAR RENINS

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 P21 with cell dimensions a = 78·3 A ̊, b = 117·8 A ̊, c = 85·9 A ̊, β = 101·18 ° 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 P213 with a = 143·1 A ̊ 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. © 1992.