4bhx
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of the SCAN domain from human paternally expressed gene 3 protein== | |
| - | + | <StructureSection load='4bhx' size='340' side='right' caption='[[4bhx]], [[Resolution|resolution]] 1.95Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BHX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bhx RCSB], [http://www.ebi.ac.uk/pdbsum/4bhx PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Eadsforth, T C | + | [[Category: Eadsforth, T C]] |
| - | [[Category: Hunter, W N | + | [[Category: Hunter, W N]] |
| - | [[Category: Rimsa, V | + | [[Category: Rimsa, V]] |
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Peg3]] | [[Category: Peg3]] | ||
Revision as of 09:49, 21 December 2014
Crystal structure of the SCAN domain from human paternally expressed gene 3 protein
| |||||||||||
