Crystal Structures of the Tricorn Interacting Factor F3 from Thermoplasma acidophilum, a Zinc Aminopeptidase in Three Different Conformations
- 26 April 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 349 (4) , 787-800
- https://doi.org/10.1016/j.jmb.2005.03.070
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanismThe EMBO Journal, 2002
- The influence of residue 190 in the S1 site of trypsin‐like serine proteases on substrate selectivity is universally conservedFEBS Letters, 2002
- Crystal structure of the tricorn protease reveals a protein disassembly lineNature, 2001
- Families of zinc metalloproteasesPublished by Wiley ,2001
- Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation.Nature Structural & Molecular Biology, 2001
- Crystal Structure of a β-Catenin/Tcf ComplexCell, 2000
- The Role of Tricorn Protease and Its Aminopeptidase-Interacting Factors in Cellular Protein DegradationCell, 1998
- Tricorn protease (TRI) interacting factor 1 from Thermoplasma acidophilum is a proline iminopeptidaseFEBS Letters, 1996
- The α/β hydrolase foldProtein Engineering, Design and Selection, 1992
- Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitorBiochemistry, 1983