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TitleAn Activity-Based Probe for Cathepsin K Imaging with Excellent Potency and Selectivity.
Journal, issue, pagesJ. Med. Chem., Vol. 64, Page 13793-13806, Year 2021
Publish dateMar 18, 2021 (structure data deposition date)
AuthorsLemke, C. / Benysek, J. / Brajtenbach, D. / Breuer, C. / Jilkova, A. / Horn, M. / Busa, M. / Ulrychova, L. / Illies, A. / Kubatzky, K.F. ...Lemke, C. / Benysek, J. / Brajtenbach, D. / Breuer, C. / Jilkova, A. / Horn, M. / Busa, M. / Ulrychova, L. / Illies, A. / Kubatzky, K.F. / Bartz, U. / Mares, M. / Gutschow, M.
External linksJ. Med. Chem. / PubMed:34473502
MethodsX-ray diffraction
Resolution1.72 - 1.8 Å
Structure data

PDB-7nxl:
Structure of human cathepsin K in complex with the acrylamide inhibitor Gu3110
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-7nxm:
Structure of human cathepsin K in complex with the selective activity-based probe Gu3416
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-UUK:
tert-butyl (1-((4-(dibenzylamino)-4-oxobutyl)amino)-4-methyl-1-oxopentan-2-yl)carbamate

ChemComp-HOH:
WATER

ChemComp-UUW:
N-(4-(dibenzylamino)-4-oxobutyl)-2-(5-(dimethylamino)pentanamido)-4-methylpentanamide

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Complex / activity-based probe / acrylamide inhibitor / inhibitor

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