1m7w
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1m7w |SIZE=350|CAPTION= <scene name='initialview01'>1m7w</scene>, resolution 2.8Å | |PDB= 1m7w |SIZE=350|CAPTION= <scene name='initialview01'>1m7w</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=DAO:LAURIC ACID'>DAO</scene> | + | |LIGAND= <scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= HNF4a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Rattus rattus]) | |GENE= HNF4a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Rattus rattus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1m7w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m7w RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Iwamoto, M.]] | [[Category: Iwamoto, M.]] | ||
[[Category: Shoelson, S E.]] | [[Category: Shoelson, S E.]] | ||
| - | [[Category: DAO]] | ||
[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:32 2008'' |
Revision as of 19:12, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | HNF4a (Rattus rattus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HNF4a ligand binding domain with bound fatty acid
Overview
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.
About this Structure
1M7W is a Single protein structure of sequence from Rattus rattus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 22:12:32 2008
