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| | <StructureSection load='2q8k' size='340' side='right'caption='[[2q8k]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='2q8k' size='340' side='right'caption='[[2q8k]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2q8k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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> | + | <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='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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA2G4, EBP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> | | <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> | | </table> |
| | == Function == | | == 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>
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bange, G]] | + | [[Category: Bange G]] |
| - | [[Category: Kowalinski, E]] | + | [[Category: Kowalinski E]] |
| - | [[Category: Sinning, I]] | + | [[Category: Sinning I]] |
| - | [[Category: Wild, K]] | + | [[Category: Wild K]] |
| - | [[Category: Ebp1]]
| + | |
| - | [[Category: Methionine aminopeptidase]]
| + | |
| - | [[Category: Pa2g4]]
| + | |
| - | [[Category: Pita-bread]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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 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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xia X, Cheng A, Lessor T, Zhang Y, Hamburger AW. Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation. J Cell Physiol. 2001 May;187(2):209-17. PMID:11268000 doi:http://dx.doi.org/10.1002/jcp.1075
- ↑ Zhang Y, Woodford N, Xia X, Hamburger AW. Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases. Nucleic Acids Res. 2003 Apr 15;31(8):2168-77. PMID:12682367
- ↑ Squatrito M, Mancino M, Donzelli M, Areces LB, Draetta GF. EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes. Oncogene. 2004 May 27;23(25):4454-65. PMID:15064750 doi:http://dx.doi.org/10.1038/sj.onc.1207579
- ↑ Zhang Y, Hamburger AW. Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1) mediated repression of androgen receptor signalling. Br J Cancer. 2005 Jan 17;92(1):140-6. PMID:15583694 doi:http://dx.doi.org/6602257
- ↑ Kowalinski E, Bange G, Bradatsch B, Hurt E, Wild K, Sinning I. The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions. FEBS Lett. 2007 Sep 18;581(23):4450-4. Epub 2007 Aug 27. PMID:17765895 doi:10.1016/j.febslet.2007.08.024
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