Structural and biochemical characterization of the wild type PCSK9-EGF(AB) complex and natural familial hypercholesterolemia mutants.

doi:10.1074/jbc.M808363200

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Community

Back to search

Article

Structural and biochemical characterization of the wild type PCSK9-EGF(AB) complex and natural familial hypercholesterolemia mutants.

The Journal of biological chemistry - 9 Jan 2009

Bottomley Matthew J, Cirillo Agostino, Orsatti Laura, Ruggeri Lionello, Fisher Timothy S, Santoro Joseph C, Cummings Richard T, Cubbon Rose M, Lo Surdo Paola, Calzetta Alessandra, Noto Alessia, Baysarowich Jennifer, Mattu Marco, Talamo Fabio, De Francesco Raffaele, Sparrow Carl P, Sitlani Ayesha, Carfí Andrea

Abstract excerpt

PCSK9 regulates low density lipoprotein receptor (LDLR) levels and consequently is a target for the prevention of atherosclerosis and coronary heart disease. Here we studied the interaction, of LDLR EGF(A/AB) repeats with PCSK9. We show that PCSK9 binds the EGF(AB) repeats in a pH-dependent manner. Although the PCSK9 C-terminal domain is not involved in LDLR binding, PCSK9 autocleavage is required. Moreover, we...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hyperlipoproteinemia Type II

Share to Proprotein Convertase 9

Share to Proprotein Convertases

Share to Protein Structure, Quaternary

Share to Protein Structure, Tertiary

Share to Receptors, LDL

Share to Serine Endopeptidases

Source

Open in PubMed

Identifiers

PMID: 19001363
DOI: 10.1074/jbc.M808363200

Genes

PCSK9
EGF
LDLR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and biochemical characterization of the wild type PCSK9-EGF(AB) complex and natural familial hypercholesterolemia mutants.PMID 19001363Read ↗

Characterization of the role of EGF-A of low density lipoprotein receptor in PCSK9 binding.Semantic proximity Read ↗

Identification and characterization of new gain-of-function mutations in the PCSK9 gene responsible for autosomal dominant hypercholesterolemia.Semantic proximity Read ↗

A transient amphipathic helix in PCSK9’s prodomain facilitates low-density lipoprotein bindingSemantic proximity Read ↗

The proprotein convertase (PC) PCSK9 is inactivated by furin and/or PC5/6A: functional consequences of natural mutations and post-translational modifications.Semantic proximity Read ↗

A transient amphipathic helix in the prodomain of PCSK9 facilitates binding to low-density lipoprotein particles.Semantic proximity Read ↗

Antagonism of secreted PCSK9 increases low density lipoprotein receptor expression in HepG2 cells.Semantic proximity Read ↗

Degradation of LDLR protein mediated by 'gain of function' PCSK9 mutants in normal and ARH cells.Semantic proximity Read ↗

Molecular basis of PCSK9 function.Semantic proximity Read ↗

Mutation S462P in the PCSK9 gene reduces secretion of mutant PCSK9 without affecting the autocatalytic cleavage.Semantic proximity Read ↗

Structural Dynamics of LDL Receptor Interactions with E498A and R499G Variants of PCSK9Semantic proximity Read ↗

In Silico Insights into Protein-protein Interaction Disruptive Mutations in the PCSK9-LDLR complex.Semantic proximity Read ↗

Interaction between the ligand-binding domain of the LDL receptor and the C-terminal domain of PCSK9 is required for PCSK9 to remain bound to the LDL receptor during endosomal acidification.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.