ArticleBiochemistry2011
The structure, dynamics, and binding of the LA45 module pair of the low-density lipoprotein receptor suggest an important role for LA4 in ligand release.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Molecular modeling of LDLR aids interpretation of genomic variants.Journal of molecular medicine (Berlin, Germany) · 2019Article
- Identification of amino acid residues in the ligand binding repeats of LDL receptor important for PCSK9 binding.Journal of lipid research · 2019Article
- Lipidated apolipoprotein E4 structure and its receptor binding mechanism determined by a combined cross-linking coupled to mass spectrometry and molecular dynamics approach.PLoS computational biology · 2018Article
- Replacement of cysteine at position 46 in the first cysteine-rich repeat of the LDL receptor impairs apolipoprotein recognition.PloS one · 2018Article
- Identification of roles for H264, H306, H439, and H635 in acid-dependent lipoprotein release by the LDL receptor.Journal of lipid research · 2017Article
- Exploring the complete mutational space of the LDL receptor LA5 domain using molecular dynamics: linking SNPs with disease phenotypes in familial hypercholesterolemia.Human molecular genetics · 2016Article
- LBD1 of Vitellogenin Receptor Specifically Binds to the Female-Specific Storage Protein SP1 via LBR1 and LBR3.PloS one · 2016Article
- Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor.PloS one · 2015Article
- Quantitative dissection of the binding contributions of ligand lysines of the receptor-associated protein (RAP) to the low density lipoprotein receptor-related protein (LRP1).The Journal of biological chemistry · 2013Article
- Mapping the binding region on the low density lipoprotein receptor for blood coagulation factor VIII.The Journal of biological chemistry · 2013Article
- Quantitative fluorescence imaging reveals point of release for lipoproteins during LDLR-dependent uptake.Journal of lipid research · 2013Article
- Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: insight from the nmr structure of the 10th complement type repeat domain alone and in complex with gentamicin.The Journal of biological chemistry · 2013Article
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2 authors at 1 institution in 1 country.
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Abstract
The low-density lipoprotein receptor (LDLR), the primary receptor for cholesterol uptake, binds ligands through its seven LDL-A modules (LAs). We present nuclear magnetic resonance (NMR) and ligand binding measurements on the fourth and fifth modules of the LDLR (LA45), the modules critical for ApoE binding, at physiological pH. Unlike LA5 and all other modules in LDLR, LA4 has a very weak calcium affinity, which probably plays a critical role in endosomal ligand release. The NMR solution structure of each module in the LA45 pair only showed minor differences compared to the analogous domains in previously determined crystal structures. The 12-residue linker connecting the modules, though slightly structured through an interaction with LA4, is highly flexible. Although no intermodule nuclear Overhauser effects were detected, chemical shift perturbations and backbone dynamics suggest cross talk between the two modules. The ligand affinity of both modules is enhanced when the two are linked. LA4 is more flexible than LA5 and remains so even in the module pair, which likely is related to its weaker calcium binding affinity.
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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.