The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA

Biochemistry
J J LovePeter E Wright

Abstract

Lymphoid enhancer-binding factor-1 (LEF-1), a member of the high-mobility group (HMG) family of proteins, functions as an architectural transcription factor. In complex with its cognate DNA, the LEF-1 domain is highly ordered, and its NMR spectra are characteristic of a folded globular protein. In contrast, the uncomplexed protein exhibits NMR evidence of substantial conformational heterogeneity, although circular dichroism spectra indicate that much of the alpha-helical secondary structure of the DNA-bound state is retained in the free protein. Heteronuclear NMR experiments performed on the free LEF-1 domain reveal that helix II and helix III of the HMG domain are folded, although helix III is truncated at its C-terminal end relative to the DNA-bound protein. The major hydrophobic core between helices II and III appears to be formed, but the minor core near the C-terminus of helix III is unstructured in the free protein. Backbone resonances of helix I are undetectable, probably as a result of exchange broadening due to fluctuations between two or more conformations on a microsecond-to-millisecond time scale. On the basis of the circular dichroism spectrum, this region of the polypeptide appears to adopt helical structure but t...Continue Reading

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