1pog

<StructureSection load='1pog' size='340' side='right'caption='[[1pog]], [[NMR_Ensembles_of_Models | 13 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1pog]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1POG FirstGlance]. <br>

</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=1pog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pog OCA], [https://pdbe.org/1pog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pog RCSB], [https://www.ebi.ac.uk/pdbsum/1pog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pog ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/PO2F1_HUMAN PO2F1_HUMAN]] Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR (By similarity). In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes.<ref>PMID:1684878</ref>

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== Publication Abstract from PubMed ==

The POU homeodomain (POUhd), a divergent member of the well-studied class of homeodomain proteins, is the C-terminal part of the bipartite POU domain, the conserved DNA-binding domain of the POU proteins. In this paper we present the solution structure of POUhd of the human Oct-1 transcription factor. This fragment was overexpressed in Escherichia coli and studied by two- and three-dimensional homo- and heteronuclear NMR techniques, resulting in virtually complete 1H and 15N resonance assignments for residues 2-60. Using distance and dihedral constraints derived from the NMR data, 50 distance geometry structures were calculated, which were refined by means of restrained molecular dynamics. From this set a total of 31 refined structures were selected, having low constraint energy and few constraint violations. The ensemble of 31 structures displays a root-mean-square deviation of the coordinates of 0.59 A with respect to the average structure, calculated over the backbone atoms of residues 6 to 54. The fold of POUhd is very similar to that of the canonical homeodomains. Interestingly, the recognition helix of the free POUhd ends at residue 53, while in the cocrystal structure of the intact POU domain with the DNA octamer motif [Klemm, J.D., Rould, M.A., Aurora, R., Herr, W. and Pabo, C.O. (1994) Cell, 77, 21-32] this helix in the POUhd subdomain is extended as far as residue 60.

Solution structure of the Oct-1 POU homeodomain determined by NMR and restrained molecular dynamics.,Cox M, van Tilborg PJ, de Laat W, Boelens R, van Leeuwen HC, van der Vliet PC, Kaptein R J Biomol NMR. 1995 Jul;6(1):23-32. PMID:7663141<ref>PMID:7663141</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1pog" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Boelens, R]]

[[Category: Cox, M]]

[[Category: Kaptein, R]]

[[Category: Laat, W De]]

[[Category: Leeuwen, H C.Van]]

[[Category: Tilborg, P J.A Van]]

[[Category: Vliet, P C.Van Der]]

[[Category: Dna binding protein]]