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BC2 nanobody in complex with the BC2 peptide tagBC2 nanobody in complex with the BC2 peptide tag
Structural highlights
FunctionPublication Abstract from PubMedNanobodies are highly valuable tools for numerous bioanalytical and biotechnical applications. Here, we report the characterization of a nanobody that binds a short peptide epitope with extraordinary affinity. Structural analysis reveals an unusual binding mode where the extended peptide becomes part of a beta-sheet structure in the nanobody. This interaction relies on sequence-independent backbone interactions augmented by a small number of specificity-determining side chain contacts. Once bound, the peptide is fastened by two nanobody side chains that clamp it in a headlock fashion. Exploiting this unusual binding mode, we generated a novel nanobody-derived capture and detection system. Matrix-coupled nanobody enables the fast and efficient isolation of epitope-tagged proteins from prokaryotic and eukaryotic expression systems. Additionally, the fluorescently labeled nanobody visualizes subcellular structures in different cellular compartments. The high-affinity-binding and modifiable peptide tag of this system renders it a versatile and robust tool to combine biochemical analysis with microscopic studies. Peptides in headlock - a novel high-affinity and versatile peptide-binding nanobody for proteomics and microscopy.,Braun MB, Traenkle B, Koch PA, Emele F, Weiss F, Poetz O, Stehle T, Rothbauer U Sci Rep. 2016 Jan 21;6:19211. doi: 10.1038/srep19211. PMID:26791954[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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