4bqa: Difference between revisions
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==Crystal structure of the ETS domain of human ETS2 in complex with DNA== | ==Crystal structure of the ETS domain of human ETS2 in complex with DNA== | ||
<StructureSection load='4bqa' size='340' side='right' caption='[[4bqa]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4bqa' size='340' side='right'caption='[[4bqa]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bqa]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BQA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BQA FirstGlance]. <br> | <table><tr><td colspan='2'>[[4bqa]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BQA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BQA FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bountra, C]] | [[Category: Bountra, C]] | ||
Revision as of 16:34, 13 March 2019
Crystal structure of the ETS domain of human ETS2 in complex with DNACrystal structure of the ETS domain of human ETS2 in complex with DNA
Structural highlights
Function[ETS2_HUMAN] Transcription factor activating transcription. Binds specifically the DNA GGAA/T core motif (Ets-binding site or EBS) in gene promoters and stimulates transcription.[1] Publication Abstract from PubMedEts-2, like its closely related homologue Ets-1, is a member of the Ets family of DNA binding transcription factors. Both proteins are subject to multiple levels of regulation of their DNA binding and transactivation properties. One such regulatory mechanism is the presence of an autoinhibitory module, which in Ets-1 allosterically inhibits the DNA binding activity. This inhibition can be relieved by interaction with protein partners or cooperative binding to closely separated Ets binding sites in a palindromic arrangement. In this study we describe the 2.5 A resolution crystal structure of a DNA complex of the Ets-2 Ets domain. The Ets domain crystallized with two distinct species in the asymmetric unit, which closely resemble the autoinhibited and DNA bound forms of Ets-1. This discovery prompted us to re-evaluate the current model for the autoinhibitory mechanism and the structural basis for cooperative DNA binding. In contrast to Ets-1, in which the autoinhibition is caused by a combination of allosteric and steric mechanisms, we were unable to find clear evidence for the allosteric mechanism in Ets-2. We also demonstrated two possibly distinct types of cooperative binding to substrates with Ets binding motifs separated by four and six base pairs and suggest possible molecular mechanisms for this behavior. Structural insights into the autoregulation and cooperativity of the human transcription factor ets-2.,Newman JA, Cooper CD, Aitkenhead H, Gileadi O J Biol Chem. 2015 Mar 27;290(13):8539-49. doi: 10.1074/jbc.M114.619270. Epub 2015, Feb 10. PMID:25670864[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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