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6i2g
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==ALFA-tag binding nanobody (NbALFA) bound to ALFA-tag peptide.== | |
| + | <StructureSection load='6i2g' size='340' side='right'caption='[[6i2g]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6i2g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vicugna_pacos Vicugna pacos] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I2G FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LPD:L-PROLINAMIDE'>LPD</scene>, <scene name='pdbligand=N7P:1-ACETYL-L-PROLINE'>N7P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6i2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i2g OCA], [https://pdbe.org/6i2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i2g RCSB], [https://www.ebi.ac.uk/pdbsum/6i2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i2g ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Specialized epitope tags are widely used for detecting, manipulating or purifying proteins, but often their versatility is limited. Here, we introduce the ALFA-tag, a rationally designed epitope tag that serves a remarkably broad spectrum of applications in life sciences while outperforming established tags like the HA-, FLAG(R)- or myc-tag. The ALFA-tag forms a small and stable alpha-helix that is functional irrespective of its position on the target protein in prokaryotic and eukaryotic hosts. We characterize a nanobody (NbALFA) binding ALFA-tagged proteins from native or fixed specimen with low picomolar affinity. It is ideally suited for super-resolution microscopy, immunoprecipitations and Western blotting, and also allows in vivo detection of proteins. We show the crystal structure of the complex that enabled us to design a nanobody mutant (NbALFA(PE)) that permits efficient one-step purifications of native ALFA-tagged proteins, complexes and even entire living cells using peptide elution under physiological conditions. | ||
| - | + | The ALFA-tag is a highly versatile tool for nanobody-based bioscience applications.,Gotzke H, Kilisch M, Martinez-Carranza M, Sograte-Idrissi S, Rajavel A, Schlichthaerle T, Engels N, Jungmann R, Stenmark P, Opazo F, Frey S Nat Commun. 2019 Sep 27;10(1):4403. doi: 10.1038/s41467-019-12301-7. PMID:31562305<ref>PMID:31562305</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6i2g" style="background-color:#fffaf0;"></div> |
| - | [[Category: Martinez-Carranza | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Vicugna pacos]] | ||
| + | [[Category: Martinez-Carranza M]] | ||
| + | [[Category: Stenmark P]] | ||
Current revision
ALFA-tag binding nanobody (NbALFA) bound to ALFA-tag peptide.
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