Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail.

doi:10.1073/pnas.1114128109

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Article

Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail.

Proceedings of the National Academy of Sciences of the United States of America - 1 May 2012

Dvir Hay, Shah Mehul, Girardi Enrico, Guo Lixia, Farquhar Marilyn G, Zajonc Dirk M

Abstract excerpt

Hypercholesterolemia, high serum cholesterol in the form of LDL, is a major risk factor for atherosclerosis. LDL is mostly degraded in the liver after its cellular internalization with the LDL receptor (LDLR). This clathrin-mediated endocytosis depends on the protein autosomal recessive hypercholesterolemia (ARH), which binds the LDLR cytoplasmic tail. Mutations in either the LDLR tail or in ARH lead to...

Topics

Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Animals
Atherosclerosis
Cholesterol, LDL
Crystallography, X-Ray
Humans
Hydrogen Bonding
Hydrophobic and Hydrophilic Interactions
Hypercholesterolemia

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

In Vitro Techniques

Models, Molecular

Molecular Sequence Data

Multiprotein Complexes

Mutation

Protein Interaction Domains and Motifs

Protein Stability

Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 22509010
DOI: 10.1073/pnas.1114128109
PMCID: PMC3344954

Genes

LDLR

Provenance

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