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 crystal structure of 1 bound to a Cys25Ser mutant of cathepsin S helped to elucidate the binding mode of a previously disclosed series of pyrazole-based CatS inhibitors and facilitated the design of a new class of arylalkyne analogs. Optimization of the alkyne and tetrahydropyridine portions of the pharmacophore provided potent CatS inhibitors (IC50=40-300 nM), and an X-ray structure of 32 revealed that the arylalkyne moiety binds in the S1 pocket of the enzyme.
Pyrazole-based cathepsin S inhibitors with arylalkynes as P1 binding elements.,Ameriks MK, Axe FU, Bembenek SD, Edwards JP, Gu Y, Karlsson L, Randal M, Sun S, Thurmond RL, Zhu J Bioorg Med Chem Lett. 2009 Nov 1;19(21):6131-4. Epub 2009 Sep 10. PMID:19773165[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ameriks MK, Axe FU, Bembenek SD, Edwards JP, Gu Y, Karlsson L, Randal M, Sun S, Thurmond RL, Zhu J. Pyrazole-based cathepsin S inhibitors with arylalkynes as P1 binding elements. Bioorg Med Chem Lett. 2009 Nov 1;19(21):6131-4. Epub 2009 Sep 10. PMID:19773165 doi:10.1016/j.bmcl.2009.09.014
