ArticleJournal of molecular biology2013
Malachite green mediates homodimerization of antibody VL domains to form a fluorescent ternary complex with singular symmetric interfaces.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 86 citations in OpenAlex.
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- Combining Machine Learning and Multiplexed,bioRxiv : the preprint server for biology · 2025Article
- Azetidinyl Malachite Green: a superior fluorogen-activating protein probe for live-cell and dynamic SIM imaging.Chemical science · 2025Article
- Biofilm dispersal patterns revealed using far-red fluorogenic probes.PLoS biology · 2024Article
- Rapid discovery and evolution of nanosensors containing fluorogenic amino acids.Nature communications · 2024Article
- Cell-cell communication: new insights and clinical implications.Signal transduction and targeted therapy · 2024Review
- Biofilm dispersal patterns revealed using far-red fluorogenic probes.bioRxiv : the preprint server for biology · 2024Article
- Optimization of the fluorogen-activating protein tag for quantitative protein trafficking and colocalization studies inMolecular biology of the cell · 2024Article
- Cutting Edge: LAG3 Dimerization Is Required for TCR/CD3 Interaction and Inhibition of Antitumor Immunity.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Symmetry-breaking malachite green as a near-infrared light-activated fluorogenic photosensitizer for RNA proximity labeling.Nucleic acids research · 2024Article
- Cell-lysis sensing drives biofilm formation in Vibrio cholerae.Nature communications · 2024Article
- Aberrant Topologies of Bacterial Membrane Proteins Revealed by High Sensitivity Fluorescence Labelling.Journal of molecular biology · 2024Article
- Computerized fluorescence microscopy of microbial cells.World journal of microbiology & biotechnology · 2021Review
- Temporally and spatially partitioned neuropeptide release from individual clock neurons.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Photophysics of a protein-bound derivative of malachite green that sensitizes the production of singlet oxygen.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
- An Evolutionary Strategy for Identification of Higher Order, Green Fluorescent Host-Guest Pairs Compatible with Living Systems.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Protein Proximity Observed Using Fluorogen Activating Protein and Dye Activated by Proximal Anchoring (FAP-DAPA) System.ACS chemical biology · 2020Article
- Visualizing GABA A Receptor Trafficking Dynamics with Fluorogenic Protein Labeling.Current protocols in neuroscience · 2020Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
We report that a symmetric small-molecule ligand mediates the assembly of antibody light chain variable domains (VLs) into a correspondent symmetric ternary complex with novel interfaces. The L5* fluorogen activating protein is a VL domain that binds malachite green (MG) dye to activate intense fluorescence. Crystallography of liganded L5* reveals a 2:1 protein:ligand complex with inclusive C2 symmetry, where MG is almost entirely encapsulated between an antiparallel arrangement of the two VL domains. Unliganded L5* VL domains crystallize as a similar antiparallel VL/VL homodimer. The complementarity-determining regions are spatially oriented to form novel VL/VL and VL/ligand interfaces that tightly constrain a propeller conformer of MG. Binding equilibrium analysis suggests highly cooperative assembly to form a very stable VL/MG/VL complex, such that MG behaves as a strong chemical inducer of dimerization. Fusion of two VL domains into a single protein tightens MG binding over 1000-fold to low picomolar affinity without altering the large binding enthalpy, suggesting that bonding interactions with ligand and restriction of domain movements make independent contributions to binding. Fluorescence activation of a symmetrical fluorogen provides a selection mechanism for the isolation and directed evolution of ternary complexes where unnatural symmetric binding interfaces are favored over canonical antibody interfaces. As exemplified by L5*, these self-reporting complexes may be useful as modulators of protein association or as high-affinity protein tags and capture reagents.
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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.