1md0: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1md0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MD0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1md0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MD0 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k79|1k79]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k79|1k79]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETS-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETS-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1md0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1md0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1md0 RCSB], [http://www.ebi.ac.uk/pdbsum/1md0 PDBsum]</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=1md0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1md0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1md0 RCSB], [http://www.ebi.ac.uk/pdbsum/1md0 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ETS1_MOUSE ETS1_MOUSE]] Transcription factor. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Garvie, C W | [[Category: Garvie, C W]] | ||
[[Category: Graves, B J | [[Category: Graves, B J]] | ||
[[Category: Pufall, M A | [[Category: Pufall, M A]] | ||
[[Category: Wolberger, C | [[Category: Wolberger, C]] | ||
[[Category: Autoinhibition]] | [[Category: Autoinhibition]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcription factor]] | [[Category: Transcription factor]] |
Revision as of 03:20, 25 December 2014
CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1
Structural highlights
Function[ETS1_MOUSE] Transcription factor. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe DNA-binding activity of the eukaryotic transcription factor Ets-1 (E26 avian erythroblastosis virus oncogene-E twenty-six) is negatively regulated by inhibitory regions that flank the ETS domain. Based on the results of solution studies, these N- and C-terminal inhibitory regions have been proposed to pack against the ETS domain and form an autoinhibitory module whose N terminus partially unfolds upon binding of Ets-1 to DNA. Mutations that disrupt autoinhibition of DNA binding also cause a structural change in the inhibitory region. We report here a crystallographic study of fragments of Ets-1 that provide structural details of the inhibitory module and the structural transition that accompanies DNA binding. The structures of free and DNA-bound Ets-1 fragments containing the ETS domain and the inhibitory regions confirm that the N-terminal inhibitory region contains two alpha-helices one of which unfolds upon Ets-1 binding to DNA. The observations from the crystal structure, coupled with mutagenesis experiments, allow us to propose a model for the inhibited form of Ets-1 and lend insight into the flexible interaction between Ets-1 and the acute myeloid leukemia 1 protein, AML1 (RUNX1). Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships.,Garvie CW, Pufall MA, Graves BJ, Wolberger C J Biol Chem. 2002 Nov 22;277(47):45529-36. Epub 2002 Sep 6. PMID:12221090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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