Folding, Calcium Binding, and Structural Characterization of a Concatemer of the First and Second Ligand-Binding Modules of the Low-Density Lipoprotein Receptor†

Biochemistry ◽  
1998 ◽  
Vol 37 (31) ◽  
pp. 10994-11002 ◽  
Author(s):  
Stephan Bieri ◽  
Annette R. Atkins ◽  
Huang T. Lee ◽  
Donald J. Winzor ◽  
Ross Smith ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Structural Characterization ◽  
Calcium Binding ◽  
Low Density Lipoprotein ◽  
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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