XRD1 Highlights
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- C1–C4 alcohol–cavitand complexes
- Cuprate Superconductor
- Jack Bean Urease
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- Carbonic Anhydrase
- PDI8CN2
- Human Legumain
- Structure of Human NAPE-PLD
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- Enhanced Green Fluorescent Protein
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- Polycyclic Aromatic Hydrocarbons
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- Crystal structure of the earthworm toxin
- Chemistry at the protein–mineral interface in L-ferritin
- Porous N-doped graphene
- Sliding of the human DNA clamp PCNA
- S1′ Pocket of Thermolysin
- microbial NLP cytolysins
- Human ubiquitin
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Page 8 of 31
Crystal structures of human legumain unveil activation mechanisms to distinct peptidase activities
 Structure and regulation of (pro-)legumain. Top-view on the AEP active site shows how Glu190 stabilizes the protonated state of Cys189 Sg.
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The cysteine protease legumain is a key player in immunity and cancer at different cellular locations, some of which are incompatible with its pH-stability. We solved the crystal structures of zymogenic and active legumain, unveiling its activation and regulation principles. Legumain contains an Asn-specific endopeptidase activity that is electrostatically released at acidic pH. Surprisingly, we uncovered a complementary proteolytic activation route, generating a carboxypeptidase activity. |
The context-dependent activation of legumain reconciles its partly conflicting moonlighting activities.
Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation; Dall E. and Brandstetter H., Proc Natl Acad Sci USA 110, 27 (2013); doi: 10.1073/pnas.1300686110 |
Last Updated on Monday, 04 July 2022 15:23
