4go6
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of HCF-1 self-association sequence 1== | |
| - | + | <StructureSection load='4go6' size='340' side='right' caption='[[4go6]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4go6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GO6 FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Homo sapiens ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), HCFC1, HCF1, HFC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4go6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4go6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4go6 RCSB], [http://www.ebi.ac.uk/pdbsum/4go6 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
[[http://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN]] X-linked nonsyndromic intellectual deficit. Mental retardation, X-linked 3 (MRX3) [MIM:[http://omim.org/entry/309541 309541]]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23000143</ref> | [[http://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN]] X-linked nonsyndromic intellectual deficit. Mental retardation, X-linked 3 (MRX3) [MIM:[http://omim.org/entry/309541 309541]]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23000143</ref> | ||
| - | + | == Function == | |
| - | ==Function== | + | |
[[http://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN]] Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes.<ref>PMID:10920196</ref> <ref>PMID:9990006</ref> <ref>PMID:10675337</ref> <ref>PMID:10629049</ref> <ref>PMID:10779346</ref> <ref>PMID:12244100</ref> <ref>PMID:14532282</ref> <ref>PMID:12670868</ref> <ref>PMID:15190068</ref> <ref>PMID:16624878</ref> <ref>PMID:17578910</ref> <ref>PMID:20018852</ref> <ref>PMID:20200153</ref> | [[http://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN]] Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes.<ref>PMID:10920196</ref> <ref>PMID:9990006</ref> <ref>PMID:10675337</ref> <ref>PMID:10629049</ref> <ref>PMID:10779346</ref> <ref>PMID:12244100</ref> <ref>PMID:14532282</ref> <ref>PMID:12670868</ref> <ref>PMID:15190068</ref> <ref>PMID:16624878</ref> <ref>PMID:17578910</ref> <ref>PMID:20018852</ref> <ref>PMID:20200153</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Host-cell factor 1 (HCF-1) is an unusual transcriptional regulator that undergoes a process of proteolytic maturation to generate N- (HCF-1(N)) and C- (HCF-1(C)) terminal subunits noncovalently associated via self-association sequence elements. Here, we present the crystal structure of the self-association sequence 1 (SAS1) including the adjacent C-terminal HCF-1 nuclear localization signal (NLS). SAS1 elements from each of the HCF-1(N) and HCF-1(C) subunits form an interdigitated fibronectin type 3 (Fn3) tandem repeat structure. We show that the C-terminal NLS recruited by the interdigitated SAS1 structure is required for effective formation of a transcriptional regulatory complex: the herpes simplex virus VP16-induced complex. Thus, HCF-1(N)-HCF-1(C) association via an integrated Fn3 structure permits an NLS to facilitate formation of a transcriptional regulatory complex. | ||
| - | + | HCF-1 self-association via an interdigitated Fn3 structure facilitates transcriptional regulatory complex formation.,Park J, Lammers F, Herr W, Song JJ Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045687<ref>PMID:23045687</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Herr, W | + | [[Category: Herr, W]] |
| - | [[Category: Lammers, F | + | [[Category: Lammers, F]] |
| - | [[Category: Park, J | + | [[Category: Park, J]] |
| - | [[Category: Song, J | + | [[Category: Song, J]] |
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Protein interaction]] | [[Category: Protein interaction]] | ||
[[Category: Tandem fibronectin repeat]] | [[Category: Tandem fibronectin repeat]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
Revision as of 11:10, 21 December 2014
Crystal structure of HCF-1 self-association sequence 1
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