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1g39
From Proteopedia
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| - | [[ | + | ==WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN== |
| + | <StructureSection load='1g39' size='340' side='right' caption='[[1g39]], [[Resolution|resolution]] 1.22Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1g39]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G39 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f93|1f93]], [[1g2y|1g2y]], [[1g2z|1g2z]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g39 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g39 RCSB], [http://www.ebi.ac.uk/pdbsum/1g39 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The N-terminal dimerization domain of the transcriptional activator hepatocyte nuclear factor-1alpha (HNF-1alpha) is essential for DNA binding and association of the transcriptional coactivator, DCoH (dimerization cofactor of HNF-1). To investigate the basis for dimerization of HNF-1 proteins, we determined the 1.2 A resolution X-ray crystal structure of the dimerization domain of HNF-1alpha (HNF-p1). Phasing was facilitated by devising a simple synthesis for Fmoc-selenomethionine and substituting leucine residues with selenomethionine. The HNF-1 dimerization domain forms a unique, four-helix bundle that is preserved with localized conformational shifts in the DCoH complex. In three different crystal forms, HNF-p1 displays subtle shifts in the conformation of the interhelix loop and the crossing angle between the amino- and carboxyl-terminal helices. In all three crystal forms, the HNF-p1 dimers pair through an exposed hydrophobic surface that also forms the binding site for DCoH. Conserved core residues in the dimerization domain of the homologous transcriptional regulator HNF-1beta rationalize the functional heterodimerization of the HNF-1alpha and HNF-1beta proteins. Mutations in HNF-1alpha are associated with maturity-onset diabetes of the young type 3 (MODY3), and the structure of HNF-p1 provides insights into the effects of three MODY3 mutations. | ||
| - | + | High-resolution structure of the HNF-1alpha dimerization domain.,Rose RB, Endrizzi JA, Cronk JD, Holton J, Alber T Biochemistry. 2000 Dec 12;39(49):15062-70. PMID:11106484<ref>PMID:11106484</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
[[Category: Cronk, J D.]] | [[Category: Cronk, J D.]] | ||
Revision as of 10:05, 28 September 2014
WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN
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