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6p79
From Proteopedia
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==Engineered single chain antibody C9+C14 ScFv== | ==Engineered single chain antibody C9+C14 ScFv== | ||
| - | <StructureSection load='6p79' size='340' side='right'caption='[[6p79]]' scene=''> | + | <StructureSection load='6p79' size='340' side='right'caption='[[6p79]], [[Resolution|resolution]] 1.58Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P79 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6p79]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P79 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.583Å</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=6p79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p79 OCA], [https://pdbe.org/6p79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p79 RCSB], [https://www.ebi.ac.uk/pdbsum/6p79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p79 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We used the molecular modeling program Rosetta to identify clusters of amino acid substitutions in antibody fragments (scFvs and scAbs) that improve global protein stability and resistance to thermal deactivation. Using this methodology, we increased the melting temperature (Tm) and resistance to heat treatment of an antibody fragment that binds to the Clostridium botulinum hemagglutinin protein (anti-HA33). Two designed antibody fragment variants with two amino acid replacement clusters, designed to stabilize local regions, were shown to have both higher Tm compared to the parental scFv and importantly, to retain full antigen binding activity after 2 hours of incubation at 70 degrees C. The crystal structure of one thermostabilized scFv variants was solved at 1.6 A and shown to be in close agreement with the RosettaAntibody model prediction. | ||
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| + | Computer-based Engineering of Thermostabilized Antibody Fragments.,Lee J, Der BS, Karamitros CS, Li W, Marshall NM, Lungu OI, Miklos AE, Xu J, Kang TH, Lee CH, Tan B, Hughes RA, Jung ST, Ippolito GC, Gray JJ, Zhang Y, Kuhlman B, Georgiou G, Ellington AD AIChE J. 2020 Mar;66(3). doi: 10.1002/aic.16864. Epub 2019 Nov 19. PMID:32336757<ref>PMID:32336757</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6p79" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Antibody 3D structures|Antibody 3D structures]] | ||
| + | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | ||
| + | *[[Sandbox 20009|Sandbox 20009]] | ||
| + | *[[3D structures of non-human antibody|3D structures of non-human antibody]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
[[Category: Li W]] | [[Category: Li W]] | ||
[[Category: Marshall N]] | [[Category: Marshall N]] | ||
[[Category: Zhang Y]] | [[Category: Zhang Y]] | ||
Current revision
Engineered single chain antibody C9+C14 ScFv
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