The α1/2 helical backbone of the prodomains defines the intrinsic inhibitory specificity in the cathepsin L-like cysteine protease subfamily
| Autor: | Klaus Schilling, Ying Lan Guo, Joachim E. Schultz, B Wiederanders, Ursula Kurz, Chin Chia Lim |
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| Rok vydání: | 2000 |
| Předmět: |
Papain family
Paramecium Cathepsin L Recombinant Fusion Proteins Molecular Sequence Data Biophysics Inhibition kinetics Cathepsin E Biology Biochemistry Cathepsin A Protein Structure Secondary Cathepsin B Cell Line Substrate Specificity Cathepsin C Structure-Activity Relationship Propeptide Cathepsin O Sequence Analysis Protein Structural Biology Cathepsin H Cathepsin L1 Endopeptidases Genetics Animals Humans Amino Acid Sequence Molecular Biology Cell Biology Cathepsins Molecular biology Protein Structure Tertiary Cysteine Endopeptidases Kinetics Specificity biology.protein |
| Zdroj: | FEBS Letters. 469:203-207 |
| ISSN: | 0014-5793 |
| Popis: | Proregions of papain-like cysteine proteases are potent and often highly selective inhibitors of their parental enzymes. The molecular basis of their selectivity is poorly understood. For two closely related members of the cathepsin L-like subfamily we established strong selectivity differences. The propeptide of cathepsin S was observed to inhibit cathepsin L with a Ki of 0.08 nM, yet cathepsin L propeptide inhibited cathepsin S only poorly. To identify the respective structural correlates we engineered chimeric propeptides and compared their inhibitory specificity with the wild-types. Specificity resided in the N-terminal part, strongly suggesting that the backbone of the prodomain was the underlying structure. |
| Databáze: | OpenAIRE |
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