1k6o

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[[Image:1k6o.gif|left|200px]]<br /><applet load="1k6o" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1k6o.gif|left|200px]]
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caption="1k6o, resolution 3.19&Aring;" />
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'''Crystal Structure of a Ternary SAP-1/SRF/c-fos SRE DNA Complex'''<br />
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{{Structure
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|PDB= 1k6o |SIZE=350|CAPTION= <scene name='initialview01'>1k6o</scene>, resolution 3.19&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= Sap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), SRF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of a Ternary SAP-1/SRF/c-fos SRE DNA Complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1K6O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6O OCA].
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1K6O is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6O OCA].
==Reference==
==Reference==
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Crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex., Mo Y, Ho W, Johnston K, Marmorstein R, J Mol Biol. 2001 Nov 30;314(3):495-506. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11846562 11846562]
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Crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex., Mo Y, Ho W, Johnston K, Marmorstein R, J Mol Biol. 2001 Nov 30;314(3):495-506. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11846562 11846562]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Mo, Y.]]
[[Category: Mo, Y.]]
[[Category: combinatorial gene regulation]]
[[Category: combinatorial gene regulation]]
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[[Category: ets proteins]]
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[[Category: ets protein]]
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[[Category: mads-box proteins]]
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[[Category: mads-box protein]]
[[Category: protein/dna complex]]
[[Category: protein/dna complex]]
[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:13:16 2008''

Revision as of 10:13, 20 March 2008


PDB ID 1k6o

Drag the structure with the mouse to rotate
, resolution 3.19Å
Gene: Sap (Homo sapiens), SRF (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of a Ternary SAP-1/SRF/c-fos SRE DNA Complex


Contents

Overview

Combinatorial DNA binding by proteins for promoter-specific gene activation is a common mode of DNA regulation in eukaryotic organisms, and occurs at the promoter of the c-fos proto-oncogene. The c-fos promoter contains a serum response element (SRE) that mediates ternary complex formation with the Ets proteins SAP-1 or Elk-1 and the MADS-box protein, serum response factor (SRF). Here, we report the crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex containing the minimal DNA-binding domains of each protein. The structure of the complex reveals that the SAP-1 monomer and SRF dimer are bound on opposite faces of the DNA, and that the DNA recognition helix of SAP-1 makes direct contact with the DNA recognition helix of one of the two SRF subunits. These interactions facilitate an 82 degrees DNA bend around SRF and a modulation of protein-DNA contacts by each protein when compared to each of the binary DNA complexes. A comparison with a recently determined complex containing SRF, an idealized DNA site, and a SAP-1 fragment containing a SRF-interacting B-box region, shows a similar overall architecture but also shows important differences. Specifically, the comparison suggests that the B-box region of the Ets protein does not significantly influence DNA recognition by either of the proteins, and that the sequence of the DNA target effects the way in which the two proteins cooperate for DNA recognition. These studies have implications for how DNA-bound SRF may modulate the DNA-binding properties of other Ets proteins such as Elk-1, and for how other Ets proteins may modulate the DNA-binding properties of other DNA-bound accessory factors to facilitate promoter-specific transcriptional responses.

Disease

Known disease associated with this structure: Osteoarthritis of hip, female-specific, susceptibility to OMIM:[605083]

About this Structure

1K6O is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex., Mo Y, Ho W, Johnston K, Marmorstein R, J Mol Biol. 2001 Nov 30;314(3):495-506. PMID:11846562

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