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4nuf
From Proteopedia
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| - | + | ==Crystal Structure of SHP/EID1== | |
| - | === | + | <StructureSection load='4nuf' size='340' side='right' caption='[[4nuf]], [[Resolution|resolution]] 2.80Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4nuf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NUF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NUF FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, malE O3O_01660, Nr0b2, Shp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4nuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nuf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nuf RCSB], [http://www.ebi.ac.uk/pdbsum/4nuf PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Small heterodimer partner (SHP) is an orphan nuclear receptor that functions as a transcriptional repressor to regulate bile acid and cholesterol homeostasis. Although the precise mechanism whereby SHP represses transcription is not known, E1A-like inhibitor of differentiation (EID1) was isolated as a SHP-interacting protein and implicated in SHP repression. Here we present the crystal structure of SHP in complex with EID1, which reveals an unexpected EID1-binding site on SHP. Unlike the classical cofactor-binding site near the C-terminal helix H12, the EID1-binding site is located at the N terminus of the receptor, where EID1 mimics helix H1 of the nuclear receptor ligand-binding domain. The residues composing the SHP-EID1 interface are highly conserved. Their mutation diminishes SHP-EID1 interactions and affects SHP repressor activity. Together, these results provide important structural insights into SHP cofactor recruitment and repressor function and reveal a conserved protein interface that is likely to have broad implications for transcriptional repression by orphan nuclear receptors. | ||
| - | + | Structural insights into gene repression by the orphan nuclear receptor SHP.,Zhi X, Zhou XE, He Y, Zechner C, Suino-Powell KM, Kliewer SA, Melcher K, Mangelsdorf DJ, Xu HE Proc Natl Acad Sci U S A. 2014 Jan 14;111(2):839-44. doi:, 10.1073/pnas.1322827111. Epub 2013 Dec 30. PMID:24379397<ref>PMID:24379397</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: He, Y | + | == References == |
| - | [[Category: Kliewer, S A | + | <references/> |
| - | [[Category: Mangelsdorf, D J | + | __TOC__ |
| - | [[Category: Melcher, K | + | </StructureSection> |
| - | [[Category: Suino-Powell, K M | + | [[Category: Lk3 transgenic mice]] |
| - | [[Category: Xu, H E | + | [[Category: He, Y]] |
| - | [[Category: Zechner, C | + | [[Category: Kliewer, S A]] |
| - | [[Category: Zhi, X | + | [[Category: Mangelsdorf, D J]] |
| - | [[Category: Zhou, X E | + | [[Category: Melcher, K]] |
| + | [[Category: Suino-Powell, K M]] | ||
| + | [[Category: Xu, H E]] | ||
| + | [[Category: Zechner, C]] | ||
| + | [[Category: Zhi, X]] | ||
| + | [[Category: Zhou, X E]] | ||
[[Category: Peptide mimicking protein helix]] | [[Category: Peptide mimicking protein helix]] | ||
[[Category: Protein-peptide complex]] | [[Category: Protein-peptide complex]] | ||
Revision as of 16:27, 21 December 2014
Crystal Structure of SHP/EID1
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