2je1
From Proteopedia
(Difference between revisions)
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<StructureSection load='2je1' size='340' side='right'caption='[[2je1]], [[Resolution|resolution]] 2.69Å' scene=''> | <StructureSection load='2je1' size='340' side='right'caption='[[2je1]], [[Resolution|resolution]] 2.69Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2je1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2je1]] 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=2JE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JE1 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2je1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2je1 OCA], [https://pdbe.org/2je1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2je1 RCSB], [https://www.ebi.ac.uk/pdbsum/2je1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2je1 ProSAT]</span></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=2je1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2je1 OCA], [https://pdbe.org/2je1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2je1 RCSB], [https://www.ebi.ac.uk/pdbsum/2je1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2je1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/AN32A_HUMAN AN32A_HUMAN] Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression.<ref>PMID:15642345</ref> <ref>PMID:10400610</ref> <ref>PMID:11360199</ref> <ref>PMID:17557114</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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/main_output.php?pdb_ID=2je1 ConSurf]. | </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=2je1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The tumor suppressor protein pp32 is highly overexpressed in many cancers of the breast and prostate, and has also been implicated in the neurodegenerative disease spinocerebellar ataxias type 1 (SCA1). Pp32 is a multifunctional protein that is involved in the regulation of transcription, apoptosis, phosphorylation, and cell cycle progression, the latter through its association with the hyperphosphorylated form of the retinoblastoma tumor suppressor. We have determined the structure of an N-terminal pp32 fragment comprising a capped leucine-rich repeat (LRR) domain, which provides insight into the structural and biochemical properties of the pp32 (Anp32) family of proteins. | ||
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| - | The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins.,Huyton T, Wolberger C Protein Sci. 2007 Jul;16(7):1308-15. Epub 2007 Jun 13. PMID:17567741<ref>PMID:17567741</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2je1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Huyton | + | [[Category: Huyton T]] |
| - | [[Category: Wolberger | + | [[Category: Wolberger C]] |
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Current revision
The crystal Structure of the tumor supressor protein pp32 (Anp32a) :structural insights into the Anp32 family of proteins
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