Structural highlights
Function
[CATS_HUMAN] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
Publication Abstract from PubMed
A series of tetrahydropyrido-pyrazole cathepsin S (CatS) inhibitors with thioether acetamide functional groups were prepared with the goal of improving upon the cellular activity of amidoethylthioethers. This Letter describes altered amide connectivity, in conjunction with changes to other binding elements, resulting in improved potency, as well as increased knowledge of the relationship between this chemotype and human CatS activity.
Thioether acetamides as P3 binding elements for tetrahydropyrido-pyrazole cathepsin S inhibitors.,Wiener DK, Lee-Dutra A, Bembenek S, Nguyen S, Thurmond RL, Sun S, Karlsson L, Grice CA, Jones TK, Edwards JP Bioorg Med Chem Lett. 2010 Apr 1;20(7):2379-82. Epub 2010 Feb 8. PMID:20188543[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wiener DK, Lee-Dutra A, Bembenek S, Nguyen S, Thurmond RL, Sun S, Karlsson L, Grice CA, Jones TK, Edwards JP. Thioether acetamides as P3 binding elements for tetrahydropyrido-pyrazole cathepsin S inhibitors. Bioorg Med Chem Lett. 2010 Apr 1;20(7):2379-82. Epub 2010 Feb 8. PMID:20188543 doi:10.1016/j.bmcl.2010.01.103
