ArticleJournal of molecular biology2011
Biochemical and structural characterization of lysophosphatidic Acid binding by a humanized monoclonal antibody.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 22 citations in OpenAlex.
- LPA/LPAR signaling drives temporomandibular disorders-like pain through regulating the expression and sensitization of PIEZO2.Science advances · 2026Article
- Antibody specificity against highly conserved membrane protein Claudin 6 driven by single atomic contact point.iScience · 2022Article
- Lysophosphatidic acid (LPA)-antibody (504B3) engagement detected by interferometry identifies off-target binding.Lipids in health and disease · 2021Article
- Ion Binding Properties of a Naturally Occurring Metalloantibody.Antibodies (Basel, Switzerland) · 2020Article
- High-affinity pan-specific monoclonal antibodies that target cysteinyl leukotrienes and show efficacy in an acute model of colitis.Journal of lipid research · 2017Article
- Drug development against the hippo pathway in mesothelioma.Translational lung cancer research · 2017Review
- A novel approach for measuring sphingosine-1-phosphate and lysophosphatidic acid binding to carrier proteins using monoclonal antibodies and the Kinetic Exclusion Assay.Journal of lipid research · 2016Article
- Recent advances in targeting the autotaxin-lysophosphatidate-lipid phosphate phosphatase axis in vivo.Journal of biomedical research · 2016Review
- A Review: Molecular Aberrations within Hippo Signaling in Bone and Soft-Tissue Sarcomas.Frontiers in oncology · 2015Review
- Crystallization and preliminary X-ray diffraction analysis of the interleukin-3 alpha receptor bound to the Fab fragment of antibody CSL362.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Regulation of the Hippo pathway and implications for anticancer drug development.Trends in pharmacological sciences · 2013Review
- Crystal structures and biochemical studies of human lysophosphatidic acid phosphatase type 6.Protein & cell · 2013Article
- The Hippo pathway and human cancer.Nature reviews. Cancer · 2013Review
- Detection of spatial correlations in protein structures and molecular complexes.Structure (London, England : 1993) · 2012Article
- Mechanism for pre-B cell loss in VH-mutant rabbits.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
- Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Lysophosphatidic acid (LPA) is a common product of glycerophospholipid metabolism and an important mediator of signal transduction. Aberrantly high LPA concentrations accompany multiple disease states. One potential approach for treatment of these diseases, therefore, is the therapeutic application of antibodies that recognize and bind LPA as their antigen. We have determined the X-ray crystal structure of an anti-LPA antibody (LT3015) Fab fragment in its antigen-free form to 2.15 Å resolution and in complex with two LPA isotypes (14:0 and 18:2) to resolutions of 1.98 and 2.51 Å, respectively. The variable CDR (complementarity-determining region) loops at the antigen binding site adopt nearly identical conformations in the free and antigen-bound crystal structures. The crystallographic models reveal that the LT3015 antibody employs both heavy- and light-chain CDR loops to create a network of eight hydrogen bonds with the glycerophosphate head group of its LPA antigen. The head group is almost completely excluded from contact with solvent, while the hydrocarbon tail is partially solvent-exposed. In general, mutation of amino acid residues at the antigen binding site disrupts LPA binding. However, the introduction of particular mutations chosen strategically on the basis of the structures can positively influence LPA binding affinity. Finally, these structures elucidate the exquisite specificity demonstrated by an anti-lipid antibody for binding a structurally simple and seemingly unconstrained target molecule.
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Registered trials
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.