1g39

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<StructureSection load='1g39' size='340' side='right'caption='[[1g39]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
<StructureSection load='1g39' size='340' side='right'caption='[[1g39]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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 [https://proteopedia.org/fgij/fg.htm?mol=1G39 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1g39]] is a 4 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=1G39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G39 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f93|1f93]], [[1g2y|1g2y]], [[1g2z|1g2z]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.22&#8491;</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=1g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g39 OCA], [https://pdbe.org/1g39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g39 RCSB], [https://www.ebi.ac.uk/pdbsum/1g39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g39 ProSAT]</span></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=1g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g39 OCA], [https://pdbe.org/1g39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g39 RCSB], [https://www.ebi.ac.uk/pdbsum/1g39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g39 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1g39" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alber, T]]
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[[Category: Mus musculus]]
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[[Category: Cronk, J D]]
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[[Category: Alber T]]
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[[Category: Endrizzi, J A]]
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[[Category: Cronk JD]]
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[[Category: Holton, J]]
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[[Category: Endrizzi JA]]
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[[Category: Rose, R B]]
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[[Category: Holton J]]
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[[Category: Dimerization domain]]
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[[Category: Rose RB]]
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[[Category: Four-helix bundle]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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Current revision

WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN

PDB ID 1g39

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