View source for 6xvi


==Crystal structure of Megabody Mb-Nb207-c7HopQ_A12==
<StructureSection load='6xvi' size='340' side='right'caption='[[6xvi]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xvi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_G27 Helicobacter pylori G27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XVI 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]] 2.596&#8491;</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=6xvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xvi OCA], [https://pdbe.org/6xvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xvi RCSB], [https://www.ebi.ac.uk/pdbsum/6xvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xvi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B5Z8H1_HELPG B5Z8H1_HELPG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nanobodies are popular and versatile tools for structural biology. They have a compact single immunoglobulin domain organization, bind target proteins with high affinities while reducing their conformational heterogeneity and stabilize multi-protein complexes. Here we demonstrate that engineered nanobodies can also help overcome two major obstacles that limit the resolution of single-particle cryo-electron microscopy reconstructions: particle size and preferential orientation at the water-air interfaces. We have developed and characterized constructs, termed megabodies, by grafting nanobodies onto selected protein scaffolds to increase their molecular weight while retaining the full antigen-binding specificity and affinity. We show that the megabody design principles are applicable to different scaffold proteins and recognition domains of compatible geometries and are amenable for efficient selection from yeast display libraries. Moreover, we demonstrate that megabodies can be used to obtain three-dimensional reconstructions for membrane proteins that suffer from severe preferential orientation or are otherwise too small to allow accurate particle alignment.

Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM.,Uchanski T, Masiulis S, Fischer B, Kalichuk V, Lopez-Sanchez U, Zarkadas E, Weckener M, Sente A, Ward P, Wohlkonig A, Zogg T, Remaut H, Naismith JH, Nury H, Vranken W, Aricescu AR, Pardon E, Steyaert J Nat Methods. 2021 Jan;18(1):60-68. doi: 10.1038/s41592-020-01001-6. Epub 2021 Jan, 6. PMID:33408403<ref>PMID:33408403</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xvi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori G27]]
[[Category: Large Structures]]
[[Category: Fischer B]]
[[Category: Steyaert J]]
[[Category: Uchanski T]]