The First Epidermal Growth Factor-like Domain of the Low-Density Lipoprotein Receptor Contains a Noncanonical Calcium Binding Site†

Biochemistry ◽  
2001 ◽  
Vol 40 (8) ◽  
pp. 2555-2563 ◽  
Author(s):  
Steven Malby ◽  
Ruth Pickering ◽  
Saurabh Saha ◽  
Rachel Smallridge ◽  
Sara Linse ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Calcium Binding ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Calcium Binding Site ◽  
Density Lipoprotein Receptor ◽  
Epidermal Growth

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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