View source for 5kql


==Co-crystal structure of LMW-PTP in complex with 2-oxo-1-phenyl-2-(phenylamino)ethanesulfonic acid==
<StructureSection load='5kql' size='340' side='right' caption='[[5kql]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kql]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KQL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6VY:(1~{S})-2-OXIDANYLIDENE-1-PHENYL-2-PHENYLAZANYL-ETHANESULFONIC+ACID'>6VY</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kqg|5kqg]], [[5kqm|5kqm]], [[5kqp|5kqp]]</td></tr>
<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=5kql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kql OCA], [http://pdbe.org/5kql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kql RCSB], [http://www.ebi.ac.uk/pdbsum/5kql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kql ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PPAC_HUMAN PPAC_HUMAN]] Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The low molecular weight protein tyrosine phosphatase (LMW-PTP) is a regulator of a number of signaling pathways and has been implicated as a potential target for oncology and diabetes/obesity. There is significant therapeutic interest in developing potent and selective inhibitors to control LMW-PTP activity. We report the discovery of a novel class of LMW-PTP inhibitors derived from sulfophenyl acetic amide (SPAA), some of which exhibit greater than 50-fold preference for LMW-PTP over a large panel of PTPs. X-ray crystallography reveals that binding of SPAA-based inhibitors induces a striking conformational change in the LMW-PTP active site, leading to the formation of a previously undisclosed hydrophobic pocket to accommodate the alpha-phenyl ring in the ligand. This induced-fit mechanism is likely a major contributor responsible for the exquisite inhibitor selectivity.

Inhibition of Low Molecular Weight Protein Tyrosine Phosphatase by an Induced-Fit Mechanism.,He R, Wang J, Yu ZH, Zhang RY, Liu S, Wu L, Zhang ZY J Med Chem. 2016 Oct 3. PMID:27676368<ref>PMID:27676368</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kql" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Wang, J]]
[[Category: Yu, Z H]]
[[Category: Zhang, Z Y]]
[[Category: Complex]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Inhibitor]]
[[Category: Lmw-ptp]]