1m7w

<StructureSection load='1m7w' size='340' side='right' caption='[[1m7w]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1m7w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_rat Black rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7W FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HNF4a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Black rat])</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=1m7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7w OCA], [http://pdbe.org/1m7w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m7w RCSB], [http://www.ebi.ac.uk/pdbsum/1m7w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7w ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/HNF4A_RAT HNF4A_RAT]] Transcriptionally controlled transcription factor. Binds to DNA sites required for the transcription of alpha 1-antitrypsin, apolipoprotein CIII, transthyretin genes and HNF1-alpha. May be essential for development of the liver, kidney and intestine.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

HNF4 alpha is an orphan member of the nuclear receptor family with prominent functions in liver, gut, kidney and pancreatic beta cells. We have solved the x-ray crystal structure of the HNF4 alpha ligand binding domain, which adopts a canonical fold. Two conformational states are present within each homodimer: an open form with alpha helix 12 (alpha 12) extended and collinear with alpha 10 and a closed form with alpha 12 folded against the body of the domain. Although the protein was crystallized without added ligands, the ligand binding pockets of both closed and open forms contain fatty acids. The carboxylic acid headgroup of the fatty acid ion pairs with the guanidinium group of Arg(226) at one end of the ligand binding pocket, while the aliphatic chain fills a long, narrow channel that is lined with hydrophobic residues. These findings suggest that fatty acids are endogenous ligands for HNF4 alpha and establish a framework for understanding how HNF4 alpha activity is enhanced by ligand binding and diminished by MODY1 mutations.

Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand.,Dhe-Paganon S, Duda K, Iwamoto M, Chi YI, Shoelson SE J Biol Chem. 2002 Oct 11;277(41):37973-6. Epub 2002 Aug 21. PMID:12193589<ref>PMID:12193589</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1m7w" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Black rat]]

[[Category: Chi, Y I]]

[[Category: Dhe-Paganon, S]]

[[Category: Duda, K]]

[[Category: Iwamoto, M]]

[[Category: Shoelson, S E]]

[[Category: Transcription factor]]