1g2z: Difference between revisions

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-[[Image:1g2z.png|left|200px]]
+==DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION==
+<StructureSection load='1g2z' size='340' side='right' caption='[[1g2z]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1g2z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G2Z FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g2y|1g2y]], [[1g39|1g39]]</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=1g2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g2z RCSB], [http://www.ebi.ac.uk/pdbsum/1g2z 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.
-{{STRUCTURE_1g2z|  PDB=1g2z  |  SCENE=  }}
+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>
-===DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_11106484}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[1g2z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2Z OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:011106484</ref><references group="xtra"/>
 [[Category: Alber, T.]]
 [[Category: Cronk, J D.]]