4r30
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Structure of human laforin dual specificity phosphatase domain== |
| - | + | <StructureSection load='4r30' size='340' side='right' caption='[[4r30]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4r30]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R30 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [http://www.ebi.ac.uk/pdbsum/4r30 PDBsum]</span></td></tr> | |
| - | + | </table> | |
| - | [[ | + | == Disease == |
| - | [[ | + | [[http://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN]] Lafora disease. The disease is caused by mutations affecting the gene represented in this entry. |
| - | [[ | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN]] Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.<ref>PMID:11001928</ref> <ref>PMID:11220751</ref> <ref>PMID:16901901</ref> <ref>PMID:18070875</ref> <ref>PMID:18617530</ref> <ref>PMID:19036738</ref> <ref>PMID:20453062</ref> <ref>PMID:23624058</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Cingolani, G]] | [[Category: Cingolani, G]] | ||
| + | [[Category: Koksal, A C]] | ||
| + | [[Category: Sankhala, R S]] | ||
| + | [[Category: Dual specificity phosphatase]] | ||
| + | [[Category: Glucan phosphatase]] | ||
| + | [[Category: Glycogen]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Malin]] | ||
Revision as of 14:52, 31 December 2014
Structure of human laforin dual specificity phosphatase domain
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