1k6o

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spinqualitylabelsall models 1k6o, resolution 3.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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

Page seeded by OCA on Mon Nov 12 17:47:58 2007