Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module

Deborah Fass, Stephen Blacklow, Peter S. Kim and James M. Berger
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Deborah Fass: Howard Hughes Medical Institute, Massachusetts Institute of Technology
Stephen Blacklow: Howard Hughes Medical Institute, Massachusetts Institute of Technology
Peter S. Kim: Howard Hughes Medical Institute, Massachusetts Institute of Technology
James M. Berger: Whitehead Institute for Biomedical Research, Nine Cambridge Center

Nature, 1997, vol. 388, issue 6643, 691-693

Abstract: Abstract The low-density lipoprotein receptor (LDLR) is responsible for the uptake of cholesterol-containing lipoprotein particles into cells1,2. The amino-terminal region of LDLR, which consists of seven tandemly repeated, ∼40-amino-acid, cysteine-rich modules (LDL-A modules), mediates binding to lipoproteins3,4. LDL-A modules are biologically ubiquitous domains, found in over 100 proteins in the sequence database5. The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to 1.7 å resolution by X-ray crystallography and presented here, contains a calcium ion coordinated by acidic residues that lie at the carboxy-terminal end of the domain and are conserved among LDL-A modules. Naturally occurring point mutations found in patients with the disease familial hypercholesterolaemia6 alter residues that directly coordinate Ca2+or that serve as scaffolding residues of LR5.

Date: 1997
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DOI: 10.1038/41798

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