Structural characterization of a short peptide fragment that mediates estrogen-receptor dimerization.
In a recent study it is suggested that a short peptide fragment within the estrogen receptor ligand-binding and dimerization domain might act as a constitutively active dimerization motif [Lees, J. A., Fawell, S. E., White, R. & Parker, M. G. (1990) Mol. Cell. Biol. 10, 5529-5531]. We used NMR and CD spectroscopies to characterize the structure and biophysical properties of a synthetic peptide comprising residues Thr500-His528 of the mouse estrogen receptor, including the putative dimerization motif. We found that residues Leu501-Asn523 form a nascent helix in water solution, whereas the C-terminal (Lys524-His528) has no propensity for alpha-helical conformation. We found no evidence for a strong homodimerization activity of the peptide. However, we observed concentration-dependent NMR chemical shifts of several residues that would be located on the same face of an alpha-helix. This observation suggests a weak, but specific dimerization/oligomerization of the peptide at millimolar concentrations.
Baumann
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Center for Structural Biochemistry, Karolinska Institutet, Sweden.
Härd
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D000595:Amino Acid Sequence; D001665:Binding Sites; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011960:Receptors, Estrogen / Q000737:chemistry*
D010446:Peptide Fragments; D011960:Receptors, Estrogen