2q8k
From Proteopedia
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| - | [[Image:2q8k.jpg|left|200px]] | ||
| - | < | + | ==The crystal structure of Ebp1== |
| - | + | <StructureSection load='2q8k' size='340' side='right'caption='[[2q8k]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2q8k]] is a 1 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=2Q8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q8K 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]] 1.6Å</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=2q8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q8k OCA], [https://pdbe.org/2q8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q8k RCSB], [https://www.ebi.ac.uk/pdbsum/2q8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q8k ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/PA2G4_HUMAN PA2G4_HUMAN] May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity).<ref>PMID:11268000</ref> <ref>PMID:12682367</ref> <ref>PMID:15064750</ref> <ref>PMID:15583694</ref> | |
| - | + | == Evolutionary Conservation == | |
| - | == | + | [[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/q8/2q8k_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=2q8k ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The ErbB-3 receptor binding protein (Ebp1) is a member of the proliferation-associated 2G4 (PA2G4) family implicated in regulation of cell growth and differentiation. Here, we report the crystal structure of the human Ebp1 at 1.6 A resolution. The protein has the conserved pita bread fold of methionine aminopeptidases, but without the characteristic enzymatic activity. Moreover, Ebp1 is known to interact with a number of proteins and RNAs involved in either transcription regulation or translation control. The structure provides insights in how Ebp1 discriminates between its different interaction partners. | The ErbB-3 receptor binding protein (Ebp1) is a member of the proliferation-associated 2G4 (PA2G4) family implicated in regulation of cell growth and differentiation. Here, we report the crystal structure of the human Ebp1 at 1.6 A resolution. The protein has the conserved pita bread fold of methionine aminopeptidases, but without the characteristic enzymatic activity. Moreover, Ebp1 is known to interact with a number of proteins and RNAs involved in either transcription regulation or translation control. The structure provides insights in how Ebp1 discriminates between its different interaction partners. | ||
| - | + | The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions.,Kowalinski E, Bange G, Bradatsch B, Hurt E, Wild K, Sinning I FEBS Lett. 2007 Sep 18;581(23):4450-4. Epub 2007 Aug 27. PMID:17765895<ref>PMID:17765895</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2q8k" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Bange | + | [[Category: Bange G]] |
| - | [[Category: Kowalinski | + | [[Category: Kowalinski E]] |
| - | [[Category: Sinning | + | [[Category: Sinning I]] |
| - | [[Category: Wild | + | [[Category: Wild K]] |
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Current revision
The crystal structure of Ebp1
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