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4bhx

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(New page: {{STRUCTURE_4bhx| PDB=4bhx | SCENE= }} ===Crystal structure of the SCAN domain from human paternally expressed gene 3 protein=== ==Function== [[http://www.uniprot.org/uniprot/PEG3_HU...)
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{{STRUCTURE_4bhx| PDB=4bhx | SCENE= }}
 
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===Crystal structure of the SCAN domain from human paternally expressed gene 3 protein===
 
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==Function==
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==Crystal structure of the SCAN domain from human paternally expressed gene 3 protein==
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[[http://www.uniprot.org/uniprot/PEG3_HUMAN PEG3_HUMAN]] Induces apoptosis in cooperation with SIAH1A. Acts as a mediator between p53/TP53 and BAX in a neuronal death pathway that is activated by DNA damage. Acts synergistically with TRAF2 and inhibits TNF induced apoptosis through activation of NF-kappa-B (By similarity). Possesses a tumor suppressing activity in glioma cells.<ref>PMID:11260267</ref>
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<StructureSection load='4bhx' size='340' side='right'caption='[[4bhx]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4bhx]] 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=4BHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHX FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhx OCA], [https://pdbe.org/4bhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bhx RCSB], [https://www.ebi.ac.uk/pdbsum/4bhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PEG3_HUMAN PEG3_HUMAN] Induces apoptosis in cooperation with SIAH1A. Acts as a mediator between p53/TP53 and BAX in a neuronal death pathway that is activated by DNA damage. Acts synergistically with TRAF2 and inhibits TNF induced apoptosis through activation of NF-kappa-B (By similarity). Possesses a tumor suppressing activity in glioma cells.<ref>PMID:11260267</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human paternally expressed gene 3 protein (PEG3) is a large multi-domain entity with diverse biological functions, including acting as a transcription factor. PEG3 contains twelve Cys2-His2 type zinc finger domains, extended regions of predicted disorder and at the N-terminus a SCAN domain. PEG3 has been identified as partner of the E3 ubiquitin-protein ligase Siah1, an association we sought to investigate. An efficient bacterial recombinant expression system of the human PEG3-SCAN domain was prepared and crystals appeared spontaneously when the protein was being concentrated after purification. The structure was determined at 1.95 A resolution and reveals a polypeptide fold of five helices in an extended configuration. An extensive dimerization interface, using almost a quarter of the solvent accessible surface, and key salt bridge interactions explain the stability of the dimer. Comparison with other SCAN domains reveals a high degree of conservation involving residues that contribute to the dimer interface. The PEG3-SCAN domain appears to constitute an assembly block, enabling PEG3 homo- or heterodimerization to control gene expression in a combinatorial fashion.
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==About this Structure==
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Structure of the SCAN Domain of Human Paternally Expressed Gene 3 Protein.,Rimsa V, Eadsforth TC, Hunter WN PLoS One. 2013 Jul 23;8(7):e69538. doi: 10.1371/journal.pone.0069538. Print 2013. PMID:23936039<ref>PMID:23936039</ref>
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[[4bhx]] is a 2 chain structure with 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=4BHX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<references group="xtra"/><references/>
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</div>
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<div class="pdbe-citations 4bhx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Eadsforth, T C.]]
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[[Category: Large Structures]]
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[[Category: Hunter, W N.]]
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[[Category: Eadsforth TC]]
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[[Category: Rimsa, V.]]
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[[Category: Hunter WN]]
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[[Category: Dna binding protein]]
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[[Category: Rimsa V]]
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[[Category: Peg3]]
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Current revision

Crystal structure of the SCAN domain from human paternally expressed gene 3 protein

PDB ID 4bhx

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