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Science 20 December 2002:
Vol. 298. no. 5602, pp. 2337 - 2339
DOI: 10.1126/science.1080669
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Perspectives

STRUCTURAL BIOLOGY:
LDL Receptor's b-Propeller Displaces LDL

Thomas L. Innerarity

The low density lipoprotein receptor (LDLR) binds to lipoprotein extracellularly and releases it in the endosome. In his Perspective, Innerarity discusses new structural work (Rudenko et al.) that shows that an interdomain interaction that occurs at low pH likely displaces ligand from the receptor in the endosome.

The author is at the Gladstone Institute of Cardiovascular Disease, San Francisco, CA 94110, USA. E-mail: tinnerarity{at}gladstone.ucsf.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Binding characteristics of a panel of monoclonal antibodies against the ligand binding domain of the human LDLr.
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Intracellular fate of LDL receptor family members depends on the cooperation between their ligand-binding and EGF domains.
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Genetic Causes of Monogenic Heterozygous Familial Hypercholesterolemia: A HuGE Prevalence Review.
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A Kelch {beta} Propeller Featuring as a G{beta} Structural Mimic: Reinventing the Wheel?.
J. Gettemans, K. Meerschaert, J. Vandekerckhove, and V. De Corte (2003)
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