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Structure of serum response factor core bound to DNA
L Pellegrini1, S Tan, T J Richmond
1Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, Zürich, Switzerland.
Nature
|August 10, 1995
Summary
Serum response factor, a MADS-domain transcription factor, integrates DNA binding and dimerization into a novel protein unit. Its structure reveals recognition of specific DNA conformations in complexes.
Area of Science:
- Molecular Biology
- Structural Biology
- Genetics
Background:
- Serum response factor (SRF) is a transcription factor within the MADS-domain protein family.
- SRF members are found across plant and animal kingdoms, indicating conserved functions.
Purpose of the Study:
- To elucidate the structural basis of SRF's DNA binding and protein-protein interactions.
- To understand how SRF recognizes specific DNA sequences.
Main Methods:
- X-ray crystallography was used to determine the structure of the SRF core in a DNA complex.
- Structural analysis focused on the integrated functions of DNA binding, dimerization, and accessory factor interaction.
Main Results:
- The X-ray crystal structure revealed a novel protein unit where DNA binding, dimerization, and accessory-factor interaction are compactly integrated.
- The study identified the intrinsic and induced conformation of the serum response element (SRE) DNA as the key feature recognized by SRF.
Conclusions:
- SRF's structure facilitates efficient integration of multiple functions into a compact unit.
- Specific DNA conformation is crucial for SRF's sequence recognition and function.