Structural highlights
Function
CATL1_HUMAN Important for the overall degradation of proteins in lysosomes.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Proteolysis of eukaryotic histone tails has emerged as an important factor in the modulation of cell-cycle progression and cellular differentiation. The recruitment of lysosomal cathepsin L to the nucleus where it mediates proteolysis of the mouse histone H3 tail has been described recently. Here, we report the three-dimensional crystal structures of a mature, inactive mutant of human cathepsin L alone and in complex with a peptide derived from histone H3. Canonical substrate-cathepsin L interactions are observed in the complex between the protease and the histone H3 peptide. Systematic analysis of the impact of posttranslational modifications at histone H3 on substrate selectivity suggests cathepsin L to be highly accommodating of all modified peptides. This is the first report of cathepsin L-histone H3 interaction and the first structural description of cathepsin L in complex with a substrate.
Structural basis for the recognition and cleavage of histone H3 by cathepsin L.,Adams-Cioaba MA, Krupa JC, Xu C, Mort JS, Min J Nat Commun. 2011 Feb;2:197. PMID:21326229[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Adams-Cioaba MA, Krupa JC, Xu C, Mort JS, Min J. Structural basis for the recognition and cleavage of histone H3 by cathepsin L. Nat Commun. 2011 Feb;2:197. PMID:21326229 doi:10.1038/ncomms1204
