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

2006 ◽  
Vol 98 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Changqing Zhao ◽  
Judith Abrams ◽  
Debra F. Skafar
Keyword(s):  
Hydrogen Bonding ◽  
Ligand Binding ◽  
Hydrophobic Interactions ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Targeted Mutation ◽  
Helix 12 ◽  
Key Residues

Solution Structure of the Ligand Binding Domain of the Fibroblast Growth Factor Receptor:  Role of Heparin in the Activation of the Receptor†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (48) ◽  
pp. 15787-15798 ◽  
Author(s):  
Kuo-Wei Hung ◽  
Thallapuranam Krishnaswamy S. Kumar ◽  
Karuppanan Muthusamy Kathir ◽  
Ping Xu ◽  
Feng Ni ◽  
...  
Keyword(s):  
Growth Factor ◽  
Ligand Binding ◽  
Fibroblast Growth Factor ◽  
Solution Structure ◽  
Fibroblast Growth Factor Receptor ◽  
Growth Factor Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Fibroblast Growth

Monitoring ligand-mediated helix 12 transitions within the human estrogen receptor α using bipartite tetracysteine display

2020 ◽  
Vol 18 (31) ◽  
pp. 6063-6071
Author(s):  
Ranju Pokhrel ◽  
Tang Tang ◽  
Justin M. Holub
Keyword(s):  
Estrogen Receptor ◽  
Ligand Binding ◽  
Estrogen Receptor Α ◽  
Fluorescent Labeling ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Human Estrogen Receptor ◽  
Helix 12

Fluorescent labeling coupled with bipartite tetracysteine display enables the surveillance of ligand-mediated helix 12 transitions within the estrogen receptor α ligand-binding domain.

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