1g2z: Difference between revisions

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-[[Image:1g2z.gif|left|200px]]<br /><applet load="1g2z" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1g2z, resolution 1.15&Aring;" />
-'''DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION'''<br />
-==Overview==
+==DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION==
-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.
+<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 with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1G2Z FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2z OCA], [https://pdbe.org/1g2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g2z RCSB], [https://www.ebi.ac.uk/pdbsum/1g2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2z ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HNF1A_MOUSE HNF1A_MOUSE] Transcriptional activator that regulates the tissue specific expression of multiple genes, especially in pancreatic islet cells and in liver. Required for the expression of several liver specific genes. Binds to the inverted palindrome 5'-GTTAATNATTAAC-3'.<ref>PMID:19289501</ref> <ref>PMID:10966642</ref>
+<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.
-==About this Structure==
+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>
-G2Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G2Z OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106484 11106484]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1g2z" style="background-color:#fffaf0;"></div>
-[[Category: Alber, T.]]
+== References ==
-[[Category: Cronk, J.D.]]
+<references/>
-[[Category: Endrizzi, J.A.]]
+__TOC__
-[[Category: Holton, J.]]
+</StructureSection>
-[[Category: Rose, R.B.]]
+[[Category: Large Structures]]
-[[Category: dimerization domain]]
+[[Category: Mus musculus]]
-[[Category: four-helix bundle]]
+[[Category: Alber T]]
-[[Category: selenomethionine]]
+[[Category: Cronk JD]]
-[[Category: transcription factor]]
+[[Category: Endrizzi JA]]
+[[Category: Holton J]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:39:30 2007''
+[[Category: Rose RB]]