8xj0: Difference between revisions
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==Crystal structure of AmFab mutant - P40C/E165C (Light chain), G10C/P210C(Heavy chain)== | |||
<StructureSection load='8xj0' size='340' side='right'caption='[[8xj0]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8xj0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XJ0 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]] 3.3Å</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=8xj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xj0 OCA], [https://pdbe.org/8xj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xj0 RCSB], [https://www.ebi.ac.uk/pdbsum/8xj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xj0 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fab is a promising format for antibody drug. Therefore, efforts have been made to improve its thermal stability for therapeutic and commercial use. So far, we have attempted to introduce a disulfide bond into the Fab fragment to improve its thermal stability and demonstrated that it is possible to do this without sacrificing its biochemical function. In this study, to develop a novel stabilization strategy for Fab, we attempted to introduce a disulfide bond between the variable and constant domains and prepared three variants of Fab; H:G10C + H:P210C, L:P40C + L:E165C, and H:G10C + H:P210C + L:P40C + L:E165C. Differential scanning calorimetry measurements showed that each of these variants had improved thermal stability. In addition, the variants with two disulfide bonds demonstrated a 6.5 degrees C increase in their denaturation temperatures compared to wild-type Fab. The introduction of disulfide bonds was confirmed by X-ray crystallography, and the variants retained their antigen-binding activity. The variants were also found to be less aggregative than the wild type. Our results demonstrate that the introduction of a disulfide bond between the variable and constant domains significantly improves the thermal stability of Fab. | |||
Stabilization of adalimumab Fab through the introduction of disulfide bonds between the variable and constant domains.,Yoshikawa M, Senda M, Nakamura H, Oda-Ueda N, Ueda T, Senda T, Ohkuri T Biochem Biophys Res Commun. 2024 Mar 12;700:149592. doi: , 10.1016/j.bbrc.2024.149592. Epub 2024 Jan 28. PMID:38295648<ref>PMID:38295648</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8xj0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Nakamura H]] | |||
[[Category: Ohkuri T]] | |||
[[Category: Senda M]] | |||
[[Category: Senda T]] | |||
[[Category: Yoshikawa M]] | |||
Latest revision as of 12:17, 30 October 2024
Crystal structure of AmFab mutant - P40C/E165C (Light chain), G10C/P210C(Heavy chain)
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