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4ny3
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4ny3 is ON HOLD Authors: Loew, C., Quistgaard, E.M., Nordlund, P. Description: Human PTPA in complex with peptide) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Human PTPA in complex with peptide== | |
| - | + | <StructureSection load='4ny3' size='340' side='right'caption='[[4ny3]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4ny3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NY3 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.797Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[https://proteopedia.org/fgij/fg.htm?mol=4ny3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ny3 OCA], [https://pdbe.org/4ny3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ny3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ny3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ny3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PTPA_HUMAN PTPA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.<ref>PMID:17333320</ref> <ref>PMID:16916641</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Loew C]] | ||
| + | [[Category: Nordlund P]] | ||
| + | [[Category: Quistgaard EM]] | ||
Current revision
Human PTPA in complex with peptide
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