1j4w: Difference between revisions

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New page: left|200px<br /> <applet load="1j4w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j4w" /> '''COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP W...
 
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[[Image:1j4w.gif|left|200px]]<br />
<applet load="1j4w" size="450" color="white" frame="true" align="right" spinBox="true"
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'''COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE'''<br />


==Overview==
==COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE==
Gene regulation can be tightly controlled by recognition of DNA, deformations that are induced by stress generated during transcription., The KH domains of the FUSE-binding protein (FBP), a regulator of c-myc, expression, bind in vivo and in vitro to the single-stranded far-upstream, element (FUSE), 1,500 base pairs upstream from the c-myc promoter. FBP, bound to FUSE acts through TFIIH at the promoter. Here we report the, solution structure of a complex between the KH3 and KH4 domains of FBP and, a 29-base single-stranded DNA from FUSE. The KH domains recognize two, sites, 9-10 bases in length, separated by 5 bases, with KH4 bound to the, 5' site and KH3 to the 3' site. The central portion of each site comprises, a tetrad of sequence 5'd-ATTC for KH4 and 5'd-TTTT for KH3. Dynamics, measurements show that the two KH domains bind as articulated modules to, single-stranded DNA, providing a flexible framework with which to, recognize transient, moving targets.
<StructureSection load='1j4w' size='340' side='right'caption='[[1j4w]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1j4w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J4W FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1j4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4w OCA], [https://pdbe.org/1j4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j4w RCSB], [https://www.ebi.ac.uk/pdbsum/1j4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j4w ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FUBP1_HUMAN FUBP1_HUMAN] Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription.<ref>PMID:8125259</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j4/1j4w_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j4w ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gene regulation can be tightly controlled by recognition of DNA deformations that are induced by stress generated during transcription. The KH domains of the FUSE-binding protein (FBP), a regulator of c-myc expression, bind in vivo and in vitro to the single-stranded far-upstream element (FUSE), 1,500 base pairs upstream from the c-myc promoter. FBP bound to FUSE acts through TFIIH at the promoter. Here we report the solution structure of a complex between the KH3 and KH4 domains of FBP and a 29-base single-stranded DNA from FUSE. The KH domains recognize two sites, 9-10 bases in length, separated by 5 bases, with KH4 bound to the 5' site and KH3 to the 3' site. The central portion of each site comprises a tetrad of sequence 5'd-ATTC for KH4 and 5'd-TTTT for KH3. Dynamics measurements show that the two KH domains bind as articulated modules to single-stranded DNA, providing a flexible framework with which to recognize transient, moving targets.


==About this Structure==
Structure and dynamics of KH domains from FBP bound to single-stranded DNA.,Braddock DT, Louis JM, Baber JL, Levens D, Clore GM Nature. 2002 Feb 28;415(6875):1051-6. PMID:11875576<ref>PMID:11875576</ref>
1J4W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J4W OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure and dynamics of KH domains from FBP bound to single-stranded DNA., Braddock DT, Louis JM, Baber JL, Levens D, Clore GM, Nature. 2002 Feb 28;415(6875):1051-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11875576 11875576]
</div>
<div class="pdbe-citations 1j4w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Braddock, D.T.]]
[[Category: Braddock DT]]
[[Category: Clore, G.M.]]
[[Category: Clore GM]]
[[Category: c-myc oncogene]]
[[Category: fbp]]
[[Category: fuse element]]
[[Category: single-stranded dna binding protein]]
[[Category: transcription factor]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:37:22 2007''

Latest revision as of 02:42, 28 December 2023

COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENECOMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE

Structural highlights

1j4w is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FUBP1_HUMAN Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription.[1]

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 PubMed

Gene regulation can be tightly controlled by recognition of DNA deformations that are induced by stress generated during transcription. The KH domains of the FUSE-binding protein (FBP), a regulator of c-myc expression, bind in vivo and in vitro to the single-stranded far-upstream element (FUSE), 1,500 base pairs upstream from the c-myc promoter. FBP bound to FUSE acts through TFIIH at the promoter. Here we report the solution structure of a complex between the KH3 and KH4 domains of FBP and a 29-base single-stranded DNA from FUSE. The KH domains recognize two sites, 9-10 bases in length, separated by 5 bases, with KH4 bound to the 5' site and KH3 to the 3' site. The central portion of each site comprises a tetrad of sequence 5'd-ATTC for KH4 and 5'd-TTTT for KH3. Dynamics measurements show that the two KH domains bind as articulated modules to single-stranded DNA, providing a flexible framework with which to recognize transient, moving targets.

Structure and dynamics of KH domains from FBP bound to single-stranded DNA.,Braddock DT, Louis JM, Baber JL, Levens D, Clore GM Nature. 2002 Feb 28;415(6875):1051-6. PMID:11875576[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Duncan R, Bazar L, Michelotti G, Tomonaga T, Krutzsch H, Avigan M, Levens D. A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif. Genes Dev. 1994 Feb 15;8(4):465-80. PMID:8125259
  2. ↑ Braddock DT, Louis JM, Baber JL, Levens D, Clore GM. Structure and dynamics of KH domains from FBP bound to single-stranded DNA. Nature. 2002 Feb 28;415(6875):1051-6. PMID:11875576 doi:10.1038/4151051a
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