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TitleReengineering of Circularly Permuted Caspase-2 to Enhance Enzyme Stability and Enable Crystallographic Studies.
Journal, issue, pagesAcs Chem. Biol., Vol. 20, Page 845-857, Year 2025
Publish dateJan 16, 2024 (structure data deposition date)
AuthorsFuller, J.L. / Shi, K. / Pockes, S. / Finzel, B.C. / Ashe, K.H. / Walters, M.A.
External linksAcs Chem. Biol. / PubMed:40117490
MethodsX-ray diffraction
Resolution1.51 - 1.96 Å
Structure data

PDB-8vp4:
Crystal Structure of JF1cpCasp2 with Peptide Inhibitor AcVDVAD-CHO
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-9c2y:
Crystal Structure of JF1cpCasp2 in complex with MUR-65
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsHYDROLASE / Caspase-2 / inhibitor / Alzheimer's disease / dimer / complex / peptidomimetic

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