ArticleJournal of molecular biology2021
N-terminal Transmembrane-Helix Epitope Tag for X-ray Crystallography and Electron Microscopy of Small Membrane Proteins.
Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 23 citations in OpenAlex.
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- Covalently constrained 'Di-Gembodies' enable parallel structure solutions by cryo-EM.Nature chemical biology · 2026Article
- Gluebodies Offer a Route To Improve Crystal Reliability and Diversity through Transferable Nanobody Mutations That Introduce Constitutive Close Contacts.ACS central science · 2025Article
- The molecular mechanism of fluoride export by the eukaryotic fluoride channel FEX.Nature communications · 2025Article
- Dynamic structures of a membrane transporter in native cellular membranes.Science advances · 2025Article
- A fiducial-assisted strategy compatible with resolving small MFS transporter structures in multiple conformations using cryo-EM.Nature communications · 2025Article
- Substrate transport and drug interaction of human thiamine transporters SLC19A2/A3.Nature communications · 2024Article
- Grafting the ALFA tag for structural studies of aquaporin Z.Journal of structural biology: X · 2024Article
- Transport of metformin metabolites by guanidinium exporters of the small multidrug resistance family.The Journal of general physiology · 2024Article
- Transport and inhibition mechanism for VMAT2-mediated synaptic vesicle loading of monoamines.Cell research · 2024Article
- Engineering of a synthetic antibody fragment for structural and functional studies of K+ channels.The Journal of general physiology · 2022Article
- Article
- A review on application of molecular simulation technology in food molecules interaction.Current research in food science · 2022Review
- Putting on molecular weight: Enabling cryo-EM structure determination of sub-100-kDa proteins.Current research in structural biology · 2022Review
- Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Inroads into Membrane Physiology through Transport Nanomachines.Journal of molecular biology · 2021Article
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Authors and funding
11 authors at 2 institutions in 1 country.
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Abstract
Structural studies of membrane proteins, especially small membrane proteins, are associated with well-known experimental challenges. Complexation with monoclonal antibody fragments is a common strategy to augment such proteins; however, generating antibody fragments that specifically bind a target protein is not trivial. Here we identify a helical epitope, from the membrane-proximal external region (MPER) of the gp41-transmembrane subunit of the HIV envelope protein, that is recognized by several well-characterized antibodies and that can be fused as a contiguous extension of the N-terminal transmembrane helix of a broad range of membrane proteins. To analyze whether this MPER-epitope tag might aid structural studies of small membrane proteins, we determined an X-ray crystal structure of a membrane protein target that does not crystallize without the aid of crystallization chaperones, the Fluc fluoride channel, fused to the MPER epitope and in complex with antibody. We also demonstrate the utility of this approach for single particle electron microscopy with Fluc and two additional small membrane proteins that represent different membrane protein folds, AdiC and GlpF. These studies show that the MPER epitope provides a structurally defined, rigid docking site for antibody fragments that is transferable among diverse membrane proteins and can be engineered without prior structural information. Antibodies that bind to the MPER epitope serve as effective crystallization chaperones and electron microscopy fiducial markers, enabling structural studies of challenging small membrane proteins.
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