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[[Image:2dil.gif|left|200px]]


{{Structure
==Solution structure of the SH3 domain of the human Proline-serine-threonine phosphatase-interacting protein 1==
|PDB= 2dil |SIZE=350|CAPTION= <scene name='initialview01'>2dil</scene>
<StructureSection load='2dil' size='340' side='right'caption='[[2dil]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2dil]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2DIL FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE= PSTPIP1, CD2BP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dil OCA], [https://pdbe.org/2dil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dil RCSB], [https://www.ebi.ac.uk/pdbsum/2dil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dil ProSAT], [https://www.topsan.org/Proteins/RSGI/2dil TOPSAN]</span></td></tr>
}}
</table>
 
== Disease ==
'''Solution structure of the SH3 domain of the human Proline-serine-threonine phosphatase-interacting protein 1'''
[https://www.uniprot.org/uniprot/PPIP1_HUMAN PPIP1_HUMAN] Defects in PSTPIP1 are the cause of PAPA syndrome (PAPAS) [MIM:[https://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>
 
== Function ==
 
[https://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>
==About this Structure==
== Evolutionary Conservation ==
2DIL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DIL OCA].  
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/2dil_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=2dil ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Inoue, M.]]
[[Category: Inoue M]]
[[Category: Kigawa, T.]]
[[Category: Kigawa T]]
[[Category: Koshiba, S.]]
[[Category: Koshiba S]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Tochio N]]
[[Category: Tochio, N.]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S.]]
[[Category: Yoneyama M]]
[[Category: Yoneyama, M.]]
[[Category: cd2-binding protein 1]]
[[Category: cell adhesion]]
[[Category: national project on protein structural and functional analyse]]
[[Category: nppsfa]]
[[Category: pest phosphatase-interacting protein 1]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: sh3 domain]]
[[Category: structural genomic]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:27:34 2008''

Latest revision as of 14:39, 22 May 2024

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

Structural highlights

2dil is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Disease

PPIP1_HUMAN Defects in PSTPIP1 are the cause of PAPA syndrome (PAPAS) [MIM: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.[1] [2]

Function

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.[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Shoham NG, Centola M, Mansfield E, Hull KM, Wood G, Wise CA, Kastner DL. Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway. Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13501-6. Epub 2003 Oct 31. PMID:14595024 doi:10.1073/pnas.2135380100
  2. ↑ Wise CA, Gillum JD, Seidman CE, Lindor NM, Veile R, Bashiardes S, Lovett M. Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder. Hum Mol Genet. 2002 Apr 15;11(8):961-9. PMID:11971877
  3. ↑ Li J, Nishizawa K, An W, Hussey RE, Lialios FE, Salgia R, Sunder-Plassmann R, Reinherz EL. A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion. EMBO J. 1998 Dec 15;17(24):7320-36. PMID:9857189 doi:10.1093/emboj/17.24.7320
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