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| - | {{Seed}} | |
| - | [[Image:3d8d.png|left|200px]] | |
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| - | <!--
| + | ==Crystal structure of the human Fe65-PTB1 domain== |
| - | The line below this paragraph, containing "STRUCTURE_3d8d", creates the "Structure Box" on the page.
| + | <StructureSection load='3d8d' size='340' side='right'caption='[[3d8d]], [[Resolution|resolution]] 2.20Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3d8d]] is a 2 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=3D8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D8D FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | -->
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> |
| - | {{STRUCTURE_3d8d| PDB=3d8d | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d8d OCA], [https://pdbe.org/3d8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d8d RCSB], [https://www.ebi.ac.uk/pdbsum/3d8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d8d ProSAT]</span></td></tr> |
| - | | + | </table> |
| - | ===Crystal structure of the human Fe65-PTB1 domain===
| + | == Function == |
| - | | + | [https://www.uniprot.org/uniprot/APBB1_HUMAN APBB1_HUMAN] Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its trancription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s).<ref>PMID:15031292</ref> <ref>PMID:18468999</ref> <ref>PMID:18922798</ref> <ref>PMID:19234442</ref> <ref>PMID:19343227</ref> |
| - | | + | == Evolutionary Conservation == |
| - | <!-- | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_18550529}}, adds the Publication Abstract to the page
| + | Check<jmol> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 18550529 is the PubMed ID number.
| + | <jmolCheckbox> |
| - | -->
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d8/3d8d_consurf.spt"</scriptWhenChecked> |
| - | {{ABSTRACT_PUBMED_18550529}}
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==About this Structure== | + | </jmolCheckbox> |
| - | 3D8D 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=3D8D OCA].
| + | </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=3d8d ConSurf]. |
| - | | + | <div style="clear:both"></div> |
| - | ==Reference== | + | == References == |
| - | Crystal structure of the human Fe65-PTB1 domain., Radzimanowski J, Ravaud S, Schlesinger S, Koch J, Beyreuther K, Sinning I, Wild K, J Biol Chem. 2008 Aug 22;283(34):23113-20. Epub 2008 Jun 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18550529 18550529]
| + | <references/> |
| - | | + | __TOC__ |
| - | Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain., Radzimanowski J, Ravaud S, Beyreuther K, Sinning I, Wild K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt, 5):382-5. Epub 2008 Apr 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18453707 18453707]
| + | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Radzimanowski, J.]] | + | [[Category: Radzimanowski J]] |
| - | [[Category: Ravaud, S.]] | + | [[Category: Ravaud S]] |
| - | [[Category: Sinning, I.]] | + | [[Category: Sinning I]] |
| - | [[Category: Wild, K.]] | + | [[Category: Wild K]] |
| - | [[Category: Alpha-beta structure]]
| + | |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Phosphotyrosine binding domain]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 19 20:11:06 2008''
| + | |
| Structural highlights
Function
APBB1_HUMAN Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its trancription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s).[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Perkinton MS, Standen CL, Lau KF, Kesavapany S, Byers HL, Ward M, McLoughlin DM, Miller CC. The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to stimulate Fe65/amyloid precursor protein nuclear signaling. J Biol Chem. 2004 May 21;279(21):22084-91. Epub 2004 Mar 18. PMID:15031292 doi:10.1074/jbc.M311479200
- ↑ Nakaya T, Kawai T, Suzuki T. Regulation of FE65 nuclear translocation and function by amyloid beta-protein precursor in osmotically stressed cells. J Biol Chem. 2008 Jul 4;283(27):19119-31. Epub 2008 May 9. PMID:18468999 doi:M801827200
- ↑ Lau KF, Chan WM, Perkinton MS, Tudor EL, Chang RC, Chan HY, McLoughlin DM, Miller CC. Dexras1 interacts with FE65 to regulate FE65-amyloid precursor protein-dependent transcription. J Biol Chem. 2008 Dec 12;283(50):34728-37. Epub 2008 Oct 15. PMID:18922798 doi:M801874200
- ↑ Cook PJ, Ju BG, Telese F, Wang X, Glass CK, Rosenfeld MG. Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions. Nature. 2009 Apr 2;458(7238):591-6. doi: 10.1038/nature07849. Epub 2009 Feb 22. PMID:19234442 doi:10.1038/nature07849
- ↑ Kajiwara Y, Akram A, Katsel P, Haroutunian V, Schmeidler J, Beecham G, Haines JL, Pericak-Vance MA, Buxbaum JD. FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4. PLoS One. 2009;4(4):e5071. doi: 10.1371/journal.pone.0005071. Epub 2009 Apr 3. PMID:19343227 doi:10.1371/journal.pone.0005071
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