Structural highlights
Publication Abstract from PubMed
Nanobodies 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
- ↑ Braun MB, Traenkle B, Koch PA, Emele F, Weiss F, Poetz O, Stehle T, Rothbauer U. Peptides in headlock - a novel high-affinity and versatile peptide-binding nanobody for proteomics and microscopy. Sci Rep. 2016 Jan 21;6:19211. doi: 10.1038/srep19211. PMID:26791954 doi:http://dx.doi.org/10.1038/srep19211
