5hdn: Difference between revisions

Latest revision as of 07:32, 9 August 2023

Crystal structure of heat shock factor1-DBD complex with ds-DNA and TtT

Structural highlights

5hdn is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.68Å
Ligands:	CIT, NA
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HSF1_HUMAN DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

References

↑ Holmberg CI, Hietakangas V, Mikhailov A, Rantanen JO, Kallio M, Meinander A, Hellman J, Morrice N, MacKintosh C, Morimoto RI, Eriksson JE, Sistonen L. Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1. EMBO J. 2001 Jul 16;20(14):3800-10. PMID:11447121 doi:https://dx.doi.org/10.1093/emboj/20.14.3800
↑ Knauf U, Newton EM, Kyriakis J, Kingston RE. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev. 1996 Nov 1;10(21):2782-93. PMID:8946918
↑ Kline MP, Morimoto RI. Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation. Mol Cell Biol. 1997 Apr;17(4):2107-15. PMID:9121459
↑ Xia W, Guo Y, Vilaboa N, Zuo J, Voellmy R. Transcriptional activation of heat shock factor HSF1 probed by phosphopeptide analysis of factor 32P-labeled in vivo. J Biol Chem. 1998 Apr 10;273(15):8749-55. PMID:9535852
↑ Guo Y, Guettouche T, Fenna M, Boellmann F, Pratt WB, Toft DO, Smith DF, Voellmy R. Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J Biol Chem. 2001 Dec 7;276(49):45791-9. Epub 2001 Oct 2. PMID:11583998 doi:https://dx.doi.org/10.1074/jbc.M105931200
↑ Soncin F, Zhang X, Chu B, Wang X, Asea A, Ann Stevenson M, Sacks DB, Calderwood SK. Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. Biochem Biophys Res Commun. 2003 Apr 4;303(2):700-6. PMID:12659875
↑ Hietakangas V, Ahlskog JK, Jakobsson AM, Hellesuo M, Sahlberg NM, Holmberg CI, Mikhailov A, Palvimo JJ, Pirkkala L, Sistonen L. Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. Mol Cell Biol. 2003 Apr;23(8):2953-68. PMID:12665592
↑ Wang X, Khaleque MA, Zhao MJ, Zhong R, Gaestel M, Calderwood SK. Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding. J Biol Chem. 2006 Jan 13;281(2):782-91. Epub 2005 Nov 8. PMID:16278218 doi:M505822200

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Holmberg CI, Hietakangas V, Mikhailov A, Rantanen JO, Kallio M, Meinander A, Hellman J, Morrice N, MacKintosh C, Morimoto RI, Eriksson JE, Sistonen L. Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1. EMBO J. 2001 Jul 16;20(14):3800-10. PMID:11447121 doi:https://dx.doi.org/10.1093/emboj/20.14.3800

[2] Knauf U, Newton EM, Kyriakis J, Kingston RE. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev. 1996 Nov 1;10(21):2782-93. PMID:8946918

[3] Kline MP, Morimoto RI. Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation. Mol Cell Biol. 1997 Apr;17(4):2107-15. PMID:9121459

[4] Xia W, Guo Y, Vilaboa N, Zuo J, Voellmy R. Transcriptional activation of heat shock factor HSF1 probed by phosphopeptide analysis of factor 32P-labeled in vivo. J Biol Chem. 1998 Apr 10;273(15):8749-55. PMID:9535852

[5] Guo Y, Guettouche T, Fenna M, Boellmann F, Pratt WB, Toft DO, Smith DF, Voellmy R. Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J Biol Chem. 2001 Dec 7;276(49):45791-9. Epub 2001 Oct 2. PMID:11583998 doi:https://dx.doi.org/10.1074/jbc.M105931200

[6] Soncin F, Zhang X, Chu B, Wang X, Asea A, Ann Stevenson M, Sacks DB, Calderwood SK. Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. Biochem Biophys Res Commun. 2003 Apr 4;303(2):700-6. PMID:12659875

[7] Hietakangas V, Ahlskog JK, Jakobsson AM, Hellesuo M, Sahlberg NM, Holmberg CI, Mikhailov A, Palvimo JJ, Pirkkala L, Sistonen L. Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. Mol Cell Biol. 2003 Apr;23(8):2953-68. PMID:12665592

[8] Wang X, Khaleque MA, Zhao MJ, Zhong R, Gaestel M, Calderwood SK. Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding. J Biol Chem. 2006 Jan 13;281(2):782-91. Epub 2005 Nov 8. PMID:16278218 doi:M505822200

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

@@ Line 1: / Line 1: @@
 ==Crystal structure of heat shock factor1-DBD complex with ds-DNA and TtT==
-<StructureSection load='5hdn' size='340' side='right' caption='[[5hdn]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
+<StructureSection load='5hdn' size='340' side='right'caption='[[5hdn]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hdn]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HDN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HDN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5hdn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HDN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hdg|5hdg]], [[5hdk|5hdk]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSF1, HSTF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5hdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hdn OCA], [https://pdbe.org/5hdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hdn RCSB], [https://www.ebi.ac.uk/pdbsum/5hdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hdn ProSAT]</span></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=5hdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hdn OCA], [http://pdbe.org/5hdn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hdn RCSB], [http://www.ebi.ac.uk/pdbsum/5hdn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hdn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HSF1_HUMAN HSF1_HUMAN]] DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.<ref>PMID:11447121</ref> <ref>PMID:8946918</ref> <ref>PMID:9121459</ref> <ref>PMID:9535852</ref> <ref>PMID:11583998</ref> <ref>PMID:12659875</ref> <ref>PMID:12665592</ref> <ref>PMID:16278218</ref>
+[https://www.uniprot.org/uniprot/HSF1_HUMAN HSF1_HUMAN] DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.<ref>PMID:11447121</ref> <ref>PMID:8946918</ref> <ref>PMID:9121459</ref> <ref>PMID:9535852</ref> <ref>PMID:11583998</ref> <ref>PMID:12659875</ref> <ref>PMID:12665592</ref> <ref>PMID:16278218</ref>
+==See Also==
+*[[Heat shock factor|Heat shock factor]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Feng, H]]
+[[Category: Large Structures]]
-[[Category: Liu, W]]
+[[Category: Feng H]]
-[[Category: Wang, D C]]
+[[Category: Liu W]]
-[[Category: Hsf1-dbd]]
+[[Category: Wang DC]]
-[[Category: Transcription]]
-[[Category: Ttt]]

5hdn: Difference between revisions

Latest revision as of 07:32, 9 August 2023

Crystal structure of heat shock factor1-DBD complex with ds-DNA and TtT

Structural highlights

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools