6CZS
Crystal structure of human pro-cathepsin H C26S mutant
Summary for 6CZS
| Entry DOI | 10.2210/pdb6czs/pdb |
| Related PRD ID | PRD_900006 |
| Descriptor | Pro-cathepsin H, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | papain family cysteine peptidase, protein degradation in lysosome, inhibitory prodomain, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 39785.34 |
| Authors | |
| Primary citation | Hao, Y.,Purtha, W.,Cortesio, C.,Rui, H.,Gu, Y.,Chen, H.,Sickmier, E.A.,Manzanillo, P.,Huang, X. Crystal structures of human procathepsin H. PLoS ONE, 13:e0200374-e0200374, 2018 Cited by PubMed Abstract: Cathepsin H is a member of the papain superfamily of lysosomal cysteine proteases. It is the only known aminopeptidase in the family and is reported to be involved in cancer and other major diseases. Like many other proteases, it is synthesized as an inactive proenzyme. Although the crystal structure of mature porcine cathepsin H revealed the binding of the mini-chain and provided structural basis for the aminopeptidase activity, detailed structural and functional information on the inhibition and activation of procathepsin H has been elusive. Here we present the crystal structures of human procathepsin H at 2.00 Å and 1.66 Å resolution. These structures allow us to explore in detail the molecular basis for the inhibition of the mature domain by the prodomain. Comparison with cathepsin H structure reveals how mini-chain reorients upon activation. We further demonstrate that procathepsin H is not auto-activated but can be trans-activated by cathepsin L. PubMed: 30044821DOI: 10.1371/journal.pone.0200374 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.66 Å) |
Structure validation
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