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A 22-amino-acid peptide restores DNA-binding activity to dimerization-defective mutants of the estrogen receptor.

作者信息

Lees J A, Fawell S E, White R, Parker M G

机构信息

Molecular Endocrinology Laboratory, Imperial Cancer Research Fund, London, United Kingdom.

出版信息

Mol Cell Biol. 1990 Oct;10(10):5529-31. doi: 10.1128/mcb.10.10.5529-5531.1990.

Abstract

We have identified residues within the estrogen receptor that are required for dimerization and high-affinity DNA binding. A 22-amino-acid peptide encompassing these residues was sufficient to restore DNA-binding activity to a mutant receptor lacking most of the hormone-binding domain. Point mutagenesis of the fusion protein confirmed that this sequence continued to mediate dimerization in a manner similar to that within the native receptor, although its position relative to the DNA-binding domain was appreciably altered.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0a22/361268/c588b27b2376/molcellb00046-0513-a.jpg

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