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
The synthesis and structure-activity relationship of a series of arylaminoethyl amide cathepsin S inhibitors are reported. Optimization of P3 and P2 groups to improve overall physicochemical properties resulted in significant improvements in oral bioavailability over early lead compounds. An X-ray structure of compound 37 bound to the active site of cathepsin S is also reported.
Synthesis and SAR of arylaminoethyl amides as noncovalent inhibitors of cathepsin S: P3 cyclic ethers.,Tully DC, Liu H, Chatterjee AK, Alper PB, Epple R, Williams JA, Roberts MJ, Woodmansee DH, Masick BT, Tumanut C, Li J, Spraggon G, Hornsby M, Chang J, Tuntland T, Hollenbeck T, Gordon P, Harris JL, Karanewsky DS Bioorg Med Chem Lett. 2006 Oct 1;16(19):5112-7. Epub 2006 Jul 28. PMID:16876402[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tully DC, Liu H, Chatterjee AK, Alper PB, Epple R, Williams JA, Roberts MJ, Woodmansee DH, Masick BT, Tumanut C, Li J, Spraggon G, Hornsby M, Chang J, Tuntland T, Hollenbeck T, Gordon P, Harris JL, Karanewsky DS. Synthesis and SAR of arylaminoethyl amides as noncovalent inhibitors of cathepsin S: P3 cyclic ethers. Bioorg Med Chem Lett. 2006 Oct 1;16(19):5112-7. Epub 2006 Jul 28. PMID:16876402 doi:http://dx.doi.org/10.1016/j.bmcl.2006.07.033
