View source for 5ivn


==BC2 nanobody in complex with the BC2 peptide tag==
<StructureSection load='5ivn' size='340' side='right'caption='[[5ivn]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ivn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IVN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IVN FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=6E4:L-GLUTAMAMIDE'>6E4</scene>, <scene name='pdbligand=N7P:1-ACETYL-L-PROLINE'>N7P</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ivn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ivn OCA], [http://pdbe.org/5ivn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ivn RCSB], [http://www.ebi.ac.uk/pdbsum/5ivn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ivn ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:26791954</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ivn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Braun, M B]]
[[Category: Stehle, T]]
[[Category: Affinity]]
[[Category: Capture]]
[[Category: Catenin]]
[[Category: Nanobody]]
[[Category: Peptide binding protein]]
[[Category: Tag]]