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3mpe

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Revision as of 09:08, 25 December 2014

Crystal structure of human Cathepsin-S C25S mutant with bound drug

Structural highlights

3mpe is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3mpf
Gene:	CTSS (Homo sapiens)
Activity:	Cathepsin S, with EC number 3.4.22.27
Resources:	FirstGlance, OCA, RCSB, PDBsum

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 pyridazin-4-one fragment 4 (hCatS IC(50)=170 microM) discovered through Tethering was modeled into cathepsin S and predicted to overlap in S2 with the tetrahydropyridinepyrazole core of a previously disclosed series of CatS inhibitors. This fragment served as a template to design pyridazin-3-one 12 (hCatS IC(50)=430 nM), which also incorporates P3 and P5 binding elements. A crystal structure of 12 bound to Cys25Ser CatS led to the synthesis of the potent diazinone isomers 22 (hCatS IC(50)=60 nM) and 27 (hCatS IC(50)=40 nM).

Diazinones as P2 replacements for pyrazole-based cathepsin S inhibitors.,Ameriks MK, Bembenek SD, Burdett MT, Choong IC, Edwards JP, Gebauer D, Gu Y, Karlsson L, Purkey HE, Staker BL, Sun S, Thurmond RL, Zhu J Bioorg Med Chem Lett. 2010 Jul 15;20(14):4060-4. Epub 2010 May 25. PMID:20541404^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ameriks MK, Bembenek SD, Burdett MT, Choong IC, Edwards JP, Gebauer D, Gu Y, Karlsson L, Purkey HE, Staker BL, Sun S, Thurmond RL, Zhu J. Diazinones as P2 replacements for pyrazole-based cathepsin S inhibitors. Bioorg Med Chem Lett. 2010 Jul 15;20(14):4060-4. Epub 2010 May 25. PMID:20541404 doi:10.1016/j.bmcl.2010.05.086

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3mpe"

@@ Line 9: / Line 9: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mpe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mpe RCSB], [http://www.ebi.ac.uk/pdbsum/3mpe PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CATS_HUMAN 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

3mpe

From Proteopedia

Revision as of 09:08, 25 December 2014

Crystal structure of human Cathepsin-S C25S mutant with bound drug

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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