3IV2
Crystal structure of mature apo-Cathepsin L C25A mutant
Summary for 3IV2
| Entry DOI | 10.2210/pdb3iv2/pdb |
| Related | 3K24 |
| Descriptor | Cathepsin L1, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | protease, mutant, apo, disulfide bond, glycoprotein, hydrolase, lysosome, thiol protease, zymogen |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 49408.20 |
| Authors | Adams-Cioaba, M.A.,Krupa, J.C.,Mort, J.S.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J. (deposition date: 2009-08-31, release date: 2010-03-23, Last modification date: 2021-10-13) |
| Primary citation | Adams-Cioaba, M.A.,Krupa, J.C.,Xu, C.,Mort, J.S.,Min, J. Structural basis for the recognition and cleavage of histone H3 by cathepsin L. Nat Commun, 2:197-197, 2011 Cited by PubMed Abstract: 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. PubMed: 21326229DOI: 10.1038/ncomms1204 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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