Functional characterization of LDL receptor missense variants located in the first cysteine-rich repeat in ligand binding domain of low density lipoprotein receptor

2017 ◽  
Vol 263 ◽  
pp. e102
Author(s):  
Haziq Siddiqi ◽  
Asier Benito ◽  
Shifa Jebari ◽  
Aitor Etxebarria ◽  
Kepa Uribe ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Low Density Lipoprotein ◽  
Functional Characterization ◽  
Ldl Receptor ◽  
Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Low Density Lipoprotein Receptor ◽  
Density Lipoprotein Receptor

Structural features of the low-density lipoprotein receptor facilitating ligand binding and release

2004 ◽  
Vol 32 (5) ◽  
pp. 721-723 ◽  
Author(s):  
N. Beglova ◽  
H. Jeon ◽  
C. Fisher ◽  
S.C. Blacklow
Keyword(s):  
Ligand Binding ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Structural Features ◽  
Low Ph ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Low Density Lipoprotein Receptor ◽  
Density Lipoprotein Receptor ◽  
Epidermal Growth

The LDLR (low-density lipoprotein receptor) is a modular protein built from several distinct structural units: LA (LDLR type-A), epidermal growth factor-like and β-propeller modules. The low pH X-ray structure of the LDLR revealed long-range intramolecular contacts between the propeller domain and the central LA repeats of the ligand-binding domain, suggesting that the receptor changes its overall shape from extended to closed, in response to pH. Here we discuss how the LDLR uses flexibility and rigidity of linkers between modules to facilitate ligand binding and low-pH ligand release.

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