2dil

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{{STRUCTURE_2dil| PDB=2dil | SCENE= }}
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==Solution structure of the SH3 domain of the human Proline-serine-threonine phosphatase-interacting protein 1==
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===Solution structure of the SH3 domain of the human Proline-serine-threonine phosphatase-interacting protein 1===
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<StructureSection load='2dil' size='340' side='right' caption='[[2dil]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[2dil]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DIL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DIL FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/PPIP1_HUMAN PPIP1_HUMAN]] Defects in PSTPIP1 are the cause of PAPA syndrome (PAPAS) [MIM:[http://omim.org/entry/604416 604416]]; also known as pyogenic sterile arthritis, pyoderma gangrenosum and acne or familial recurrent arthritis (FRA). PAPAS is characterized by autosomal dominant inheritance of early onset, primarily affecting skin and joint tissues. Recurring inflammatory episodes lead to accumulation of sterile, pyogenic, neutrophil-rich material within the affected joints, ultimately resulting in significant destruction.<ref>PMID:14595024</ref><ref>PMID:11971877</ref>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSTPIP1, CD2BP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dil OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dil RCSB], [http://www.ebi.ac.uk/pdbsum/2dil PDBsum], [http://www.topsan.org/Proteins/RSGI/2dil TOPSAN]</span></td></tr>
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==Function==
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<table>
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[[http://www.uniprot.org/uniprot/PPIP1_HUMAN PPIP1_HUMAN]] Involved in regulation of the actin cytoskeleton. May regulate the WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to the ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allows PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2.<ref>PMID:9857189</ref>
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== Disease ==
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[[http://www.uniprot.org/uniprot/PPIP1_HUMAN PPIP1_HUMAN]] Defects in PSTPIP1 are the cause of PAPA syndrome (PAPAS) [MIM:[http://omim.org/entry/604416 604416]]; also known as pyogenic sterile arthritis, pyoderma gangrenosum and acne or familial recurrent arthritis (FRA). PAPAS is characterized by autosomal dominant inheritance of early onset, primarily affecting skin and joint tissues. Recurring inflammatory episodes lead to accumulation of sterile, pyogenic, neutrophil-rich material within the affected joints, ultimately resulting in significant destruction.<ref>PMID:14595024</ref> <ref>PMID:11971877</ref>
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==About this Structure==
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== Function ==
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[[2dil]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DIL OCA].
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[[http://www.uniprot.org/uniprot/PPIP1_HUMAN PPIP1_HUMAN]] Involved in regulation of the actin cytoskeleton. May regulate the WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to the ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allows PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2.<ref>PMID:9857189</ref>
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== Evolutionary Conservation ==
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==Reference==
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[[Image:Consurf_key_small.gif|200px|right]]
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<references group="xtra"/><references/>
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/2dil_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Inoue, M.]]
[[Category: Inoue, M.]]

Revision as of 01:37, 30 September 2014

Solution structure of the SH3 domain of the human Proline-serine-threonine phosphatase-interacting protein 1

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