ArticleThe Journal of biological chemistry2017
Recombinant Expression of the Full-length Ectodomain of LDL Receptor-related Protein 1 (LRP1) Unravels pH-dependent Conformational Changes and the Stoichiometry of Binding with Receptor-associated Protein (RAP).
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- High-Throughput Screening Identifies Small-Molecule Inhibitors of the Tau-LRP1 Interaction.bioRxiv : the preprint server for biology · 2026Article
- A computational analysis of the glycoprotein lipoprotein receptor-related protein 1 structure and the role of glycans as quaternary glue.Bioinformatics (Oxford, England) · 2026Article
- Decoding the Mechanism of Action of a Parasite TGFβ Antagonist Inspires the Creation of Cell-Type-Specific TGFβ Modulators.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The ligand preference of LRP1 is regulated by O-glycans.Science advances · 2026Article
- Integrative structural analysis of the human LRP2-LRPAP1 complex reveals multiple regulatory sites.Communications biology · 2026Article
- Article
- LRPAP1 is released from activated microglia and inhibits microglial phagocytosis and amyloid beta aggregation.Frontiers in immunology · 2023Article
- Article
- Complement C1q Interacts With LRP1 Clusters II and IV Through a Site Close but Different From the Binding Site of Its C1r and C1s-Associated Proteases.Frontiers in immunology · 2020Article
- Bispecific, T-Cell-Recruiting Antibodies in B-Cell Malignancies.Frontiers in immunology · 2020Review
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- PhoX: An IMAC-Enrichable Cross-Linking Reagent.ACS central science · 2019Article
- Site-specificThe Journal of biological chemistry · 2018Article
- Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release.Nature communications · 2017Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LDL receptor-related protein 1 (LRP1) is a highly modular protein and the largest known mammalian endocytic receptor. LRP1 binds and internalizes many plasma components, playing multiple crucial roles as a scavenger and signaling molecule. One major challenge to studying LRP1 has been that it is difficult to express such a large, highly glycosylated, and cysteine-rich protein, limiting structural studies to LRP1 fragments. Here, we report the first recombinant expression of the complete 61 domains of the full-length LRP1 ectodomain. This advance was achieved with a multistep cloning approach and by using DNA dilutions to improve protein yields. We investigated the binding properties of LRP1 using receptor-associated protein (RAP) as a model ligand due to its tight binding interaction. The LRP1 conformation was studied in its bound and unbound state using mass spectrometry, small-angle X-ray scattering, and negative-stain electron microscopy at neutral and acidic pH. Our findings revealed a pH-dependent release of the ligand associated with a conformational change of the receptor. In summary, this investigation of the complete LRP1 ectodomain significantly advances our understanding of this important receptor and provides the basis for further elucidating the mechanism of action of LRP1 in a whole and integrated system.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.