Targeted mutation of key residues at the start of helix 12 in the hERalpha ligand-binding domain identifies the role of hydrogen-bonding and hydrophobic interactions in the activity of the protein.

Zhao, Changqing

Targeted mutation of key residues at the start of helix 12 in the hERalpha ligand-binding domain identifies the role of hydrogen-bonding and hydrophobic interactions in the activity of the protein. [electronic resource] - The Journal of steroid biochemistry and molecular biology Jan 2006 - 1-11 p. digital

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't

0960-0760

10.1016/j.jsbmb.2005.06.036 doi


Binding Sites
Estradiol--pharmacology
Estrogen Antagonists--pharmacology
Estrogen Receptor alpha--chemistry
Estrogen Receptor beta--chemistry
HeLa Cells
Humans
Hydrogen Bonding
Hydrophobic and Hydrophilic Interactions
Ligands
Models, Molecular
Mutation
Promoter Regions, Genetic--genetics
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Response Elements--genetics
Tamoxifen--analogs & derivatives
Transcription Factor AP-1--metabolism
Transcriptional Activation
Two-Hybrid System Techniques