1md0: Difference between revisions
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[[Image:1md0.gif|left|200px]] | [[Image:1md0.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1''' | {{Structure | ||
|PDB= 1md0 |SIZE=350|CAPTION= <scene name='initialview01'>1md0</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= ETS-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MD0 is a [ | 1MD0 is a [[Single protein]] structure of 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]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12221090 12221090] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:57 2008'' | ||
Revision as of 13:41, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Gene: | ETS-1 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1
OverviewOverview
The 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).
About this StructureAbout this Structure
1MD0 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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
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