View source for 9kat


==Crystal structure of anti-sulfonylurea antibody scFv apo form==
<StructureSection load='9kat' size='340' side='right'caption='[[9kat]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9kat]] 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=9KAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KAT 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]] 1.51&#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=9kat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9kat OCA], [https://pdbe.org/9kat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9kat RCSB], [https://www.ebi.ac.uk/pdbsum/9kat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9kat ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The limited understanding of the broad-specific antibody recognition mechanism significantly hinders the development of immunoassays for simultaneously detecting illegal adulterants. Herein, a recombinant antisulfonylureas (SUs) single-chain variable fragment (scFv), which retained the properties of its parental monoclonal antibody, was successfully generated. X-ray crystallography, molecular docking, functional assays, and mutation validation were used to investigate the structure-function relationships underlying antibody-SUs binding. Our study revealed three key mechanisms for broad specificity: (1) the conformational adaptability of the scFv, which enabled various SUs to access the binding pocket; (2) the role of the Trp98 residue in CDR-L3 in modulating binding affinities among multiple SUs; and (3) the design of haptens with common structures and more rigid R substituents, which emerged as a promising strategy for generating broad-specific antibodies. This study provides a comprehensive analysis of the broad-specific recognition mechanism, offering valuable insights for rational hapten design and targeted antibody evolution to advance multitarget immunoassays.

Structure Profiling of Broad-Specificity Immunoassays: Multitarget Recognition for Sulfonylurea Adulteration in Food.,Yu X, Zhou T, Pan K, Fan MH, Yan X, Huang XA, Zhang H, Shen X, Xie H, Gao YG, Lei H J Agric Food Chem. 2025 Apr 16;73(15):9348-9358. doi: 10.1021/acs.jafc.5c00655. , Epub 2025 Apr 2. PMID:40173361<ref>PMID:40173361</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9kat" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Gao YG]]
[[Category: Lei HT]]
[[Category: Yu XT]]