5kqg

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'''Unreleased structure'''
 
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The entry 5kqg is ON HOLD until Paper Publication
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==Co-crystal structure of LMW-PTP in complex with 2-(benzothiazol-2-ylamino)-2-oxo-1-phenylethanesulfonic acid==
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<StructureSection load='5kqg' size='340' side='right' caption='[[5kqg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5kqg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KQG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6VX:(1~{S})-2-(1,3-BENZOTHIAZOL-2-YLAMINO)-2-OXIDANYLIDENE-1-PHENYL-ETHANESULFONIC+ACID'>6VX</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kql|5kql]], [[5kqm|5kqm]], [[5kqp|5kqp]]</td></tr>
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<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=5kqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kqg OCA], [http://pdbe.org/5kqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kqg RCSB], [http://www.ebi.ac.uk/pdbsum/5kqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kqg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5kqg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Wang, J]]
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[[Category: Yu, Z H]]
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[[Category: Zhang, Z Y]]
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[[Category: Complex]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Inhibitor]]
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[[Category: Lmw-ptp]]

Revision as of 17:44, 19 October 2016

Co-crystal structure of LMW-PTP in complex with 2-(benzothiazol-2-ylamino)-2-oxo-1-phenylethanesulfonic acid

5kqg, resolution 1.50Å

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