Inhibitor binding induces structural changes in porcine pepsin.

作者: Cele Abad-Zapatero , T. J. Rydel , D. J. Neidhart , J. Luly , J. W. Erickson

DOI: 10.1007/978-1-4684-6012-4_2

关键词:

摘要: Crystal structures of several fungal aspartic proteinases have been refined at high resolution: penicillopepsin1, Endothia parasitica pepsin2 and Rhizopus chinensis protease.3 The structure a recombinant form human renin has solved4 2.5 A the two other mammalian reported recently: chymosin 2.3 resolution5, monoclinic porcine pepsin 1.8 resolution6,7, as well original hexagonal crystal form8.

参考文章(19)
T.L. Blundell, J.A. Jenkins, B.T. Sewell, L.H. Pearl, J.B. Cooper, I.J. Tickle, B. Veerapandian, S.P. Wood, X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin. Journal of Molecular Biology. ,vol. 211, pp. 919- 941 ,(1994) , 10.1016/0022-2836(90)90084-Y
M G Rossmann, P Argos, A comparison of the heme binding pocket in globins and cytochrome b5. Journal of Biological Chemistry. ,vol. 250, pp. 7525- 7532 ,(1975) , 10.1016/S0021-9258(19)40974-5
J.B. Cooper, G. Khan, G. Taylor, I.J. Tickle, T.L. Blundell, X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution. Journal of Molecular Biology. ,vol. 214, pp. 199- 222 ,(1990) , 10.1016/0022-2836(90)90156-G
Frances C. Bernstein, Thomas F. Koetzle, Graheme J.B. Williams, Edgar F. Meyer, Michael D. Brice, John R. Rodgers, Olga Kennard, Takehiko Shimanouchi, Mitsuo Tasumi, The Protein Data Bank: a computer-based archival file for macromolecular structures. Journal of Molecular Biology. ,vol. 112, pp. 535- 542 ,(1977) , 10.1016/S0022-2836(77)80200-3
C. Abad-Zapatero, T. J. O'Donnell, TABLES, a program to display space-group symmetry information in three dimensions Journal of Applied Crystallography. ,vol. 20, pp. 532- 535 ,(1987) , 10.1107/S0021889887086060
Gary L. Gilliland, Evon L. Winborne, Joseph Nachman, Alexander Wlodawer, The three‐dimensional structure of recombinant bovine chymosin at 2.3 Å resolution Proteins. ,vol. 8, pp. 82- 101 ,(1990) , 10.1002/PROT.340080110
M. N. James, A. Sielecki, F. Salituro, D. H. Rich, T. Hofmann, Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 79, pp. 6137- 6141 ,(1982) , 10.1073/PNAS.79.20.6137
K. Suguna, E. A. Padlan, C. W. Smith, W. D. Carlson, D. R. Davies, Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action Proceedings of the National Academy of Sciences of the United States of America. ,vol. 84, pp. 7009- 7013 ,(1987) , 10.1073/PNAS.84.20.7009