scholarly journals Estradiol (E2) Regulation And ERα, C/EBPβ And SP1 Interactions Are Essential For Human Prolactin Receptor (hPRLR) Gene Transcription In a Live Cell‐Based System

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Jung‐Hoon Kang ◽  
Chon‐Hwa Tsai‐Morris ◽  
Maria L. Dufau
2003 ◽  
Vol 278 (35) ◽  
pp. 32929-32935 ◽  
Author(s):  
Monilola A. Olayioye ◽  
Mark A. Guthridge ◽  
Frank C. Stomski ◽  
Angel F. Lopez ◽  
Jane E. Visvader ◽  
...  

Endocrinology ◽  
1998 ◽  
Vol 139 (2) ◽  
pp. 609-616 ◽  
Author(s):  
Tian-Jian Chen ◽  
Chiaoyun Benson Kuo ◽  
Kolistin F. Tsai ◽  
Jo-Wen Liu ◽  
Dih-Yih Chen ◽  
...  

2013 ◽  
Vol 13 (1) ◽  
pp. 207-222 ◽  
Author(s):  
Lin Wang ◽  
Shawn Witham ◽  
Zhe Zhang ◽  
Lin Li ◽  
Michael Hodsdon ◽  
...  

AbstractExperimental data shows that the binding of human prolactin (hPRL) to human prolactin receptor (hPRLr-ECD) is strongly pH-dependent, while the binding of the same receptor to human growth hormone (hGH) is pH-independent. Here we carry in silico analysis of the molecular effects causing such a difference and reveal the role of individual amino acids. It is shown that the computational modeling correctly predicts experimentally determined pKa’s of histidine residues in an unbound state in the majority of the cases and the pH-dependence of the binding free energy. Structural analysis carried in conjunction with calculated pH-dependence of the binding revealed that the main reason for pH-dependence of the binding of hPRL-hPRLr-ECD is a number of salt-bridges across the interface of the complex, while no salt-bridges are formed in the hGH-hPRlr-ECD. Specifically, most of the salt-bridges involve histidine residues and this is the reason for the pH-dependence across a physiological range of pH. The analysis not only revealed the molecular mechanism of the pH-dependence of the hPRL-hPRLr-ECD, but also provided critical insight into the underlying physic-chemical mechanism.


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