Adaptation of the behaviour of an aspartic proteinase inhibitor by relocation of a lysine residue by one helical turn

Biological Chemistry

Volumn 387, Issue 8, 2006, Pages 1139-1142

  Winterburn, Tim J ^a   Wyatt, David M ^a   Phylip, Lowri H ^a   Berry, Colin ^a   Bur, Daniel ^b   Kay, John ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

^b ACTELION PHARMACEUTICALS LTD   (Switzerland)

Author keywords

Amphipathic helix; Extrinsic intrinsic inhibitors of aspartic proteinases; Gastric zymogen proparts; Lysine superposition; pH dependence of interaction; Yeast IA3 inhibitor

Indexed keywords

ASPARTIC PROTEINASE INHIBITOR; ENZYME PRECURSOR; FUNGAL PROTEIN; LYSINE; POLYPEPTIDE; PROTEIN IA 3; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEINASE INHIBITION; SACCHAROMYCES CEREVISIAE;

ADAPTATION, PHYSIOLOGICAL; ASPARTIC ACID; ASPARTIC ACID ENDOPEPTIDASES; ASPARTIC ENDOPEPTIDASES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HYDROGEN-ION CONCENTRATION; LYSINE; MODELS, MOLECULAR; PROTEASE INHIBITORS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

SACCHAROMYCES CEREVISIAE;

EID: 33746907152     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2006.140     Document Type: Article

References (15)

1. Bernstein, N.K., Cherney, M.M., Loetscher, H., Ridley, R.G., and James, M.N.G. (1999). Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from P. falciparum. Nat. Struct. Biol. 6, 32-37.
2. Brik, A. and Wong, C.-H. (2003). HIV-1 protease: mechanism and drug discovery. Org. Biomol. Chem. 1, 5-14.
3. Dunn, B.M. (2002). Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem. Rev. 102, 4431-4458.
4. 3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution. Biochemistry 43, 4071-4081.
5. Gribouval, O., Gonzales, M., Neuhaus, T., Aziza, J., Bieth, E., Laurent, N., Bouton, J.M., Feuillet, F., Makni, S., Amar, H.B., et al. (2005). Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis. Nat. Genet. 37, 964-968.
6. Khan, A.R. and James, M.N.G. (1998). Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Protein Sci. 7, 815-836.
7. Lee, A.Y., Gulnik, S.V., and Erickson, J.W. (1998). Conformational switching in an aspartic proteinase. Nat. Struct. Biol. 5, 866-870.
8. Li, M., Phylip, L.H., Lees, W.E., Winther, J.R., Dunn, B.M., Wlodawer, A., Kay, J., and Gustchina, A. (2000). The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. Nat. Struct. Biol. 7, 113-117.
9. Moore, S.A., Sielecki, A.R., Chernaia, M.M., Tarasova, N.I., and James, M.N.G. (1995). Crystal and molecular structures of human progastricsin at 1.62 Å resolution. J. Mol. Biol. 247, 466-485.
10. Ng, K.K.S., Petersen, J.F.W., Cherney, M.M., Garen, C., Zalatoris, J.J., Rao-Naik, C., Dunn, B.M., Martzen, M.R., Peanasky, R.J., and James, M.N.G. (2000). Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3. Nat. Struct. Biol. 7, 653-657.
11. Oefner, C., Binggeli, A., Breu, V., Bur, D., Clozel, J.-P., D'Arcy, A., Dorn, A., Fischli, W., Gruninger, F., Guller, R., et al. (1999). Renin inhibition by substituted piperidines: a novel paradigm for the inhibition of monomeric aspartic proteinases? Chem. Biol. 6, 127-131.
12. 3 and its target aspartic proteinase. J. Biol. Chem. 276, 2023-2030.
13. ten Have, A., Dekkers, E., Kay, J., Phylip, L.H., and van Kan, J.A.L. (2004). An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features. Microbiology 150, 2475-2489.
14. Tigue, N.J. and Kay, J. (1998). Autoprocessing and peptide substrates for human herpesvirus 6 proteinase. J. Biol. Chem. 273, 26441-26446.
15. Wood, J.M., Maibaum, J., Rahuel, J., Grutter, M.G., Cohen, N-C., Rasetti, V., Ruger, H., Goschke, R., Stutz, S., Fuhrer, W., et al. (2003). Structure-based design of aliskiren, a novel orally effective renin inhibitor. Biochem. Biophys. Res. Commun. 308, 698-705.