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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A series of N(alpha)-2-benzoxazolyl-alpha-amino acid-(arylaminoethyl)amides were identified as potent, selective, and noncovalent inhibitors of cathepsin S. Structure-activity relationships including strategies for modulating the selectivities among cathepsins S, K, and L, and in vivo pharmacokinetics are discussed. A X-ray structure of compound 3 bound to the active site of cathepsin S is also reported.
Synthesis and evaluation of arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 3: heterocyclic P3.,Tully DC, Liu H, Alper PB, Chatterjee AK, Epple R, Roberts MJ, Williams JA, Nguyen KT, Woodmansee DH, Tumanut C, Li J, Spraggon G, Chang J, Tuntland T, Harris JL, Karanewsky DS Bioorg Med Chem Lett. 2006 Apr 1;16(7):1975-80. Epub 2006 Jan 30. PMID:16446091[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tully DC, Liu H, Alper PB, Chatterjee AK, Epple R, Roberts MJ, Williams JA, Nguyen KT, Woodmansee DH, Tumanut C, Li J, Spraggon G, Chang J, Tuntland T, Harris JL, Karanewsky DS. Synthesis and evaluation of arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 3: heterocyclic P3. Bioorg Med Chem Lett. 2006 Apr 1;16(7):1975-80. Epub 2006 Jan 30. PMID:16446091 doi:http://dx.doi.org/10.1016/j.bmcl.2005.12.095
