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==Crystal structure of an antibody light chain tetramer with 3D domain swapping==
<StructureSection load='8kad' size='340' side='right'caption='[[8kad]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8kad]] is a 2 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=8KAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8KAD 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&#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=8kad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8kad OCA], [https://pdbe.org/8kad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8kad RCSB], [https://www.ebi.ac.uk/pdbsum/8kad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8kad ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Overexpression of antibody light chains in small plasma cell clones can lead to misfolding and aggregation. On the other hand, the formation of amyloid fibrils from antibody light chains is related to amyloidosis. Although aggregation of antibody light chain is an important issue, atomic-level structural examinations of antibody light chain aggregates are sparse. In this study, we present an antibody light chain that maintains an equilibrium between its monomeric and tetrameric states. According to data from X-ray crystallography, thermodynamic and kinetic measurements, as well as theoretical studies, this antibody light chain engages in 3D domain swapping within its variable region. Here, a pair of domain-swapped dimers creates a tetramer through hydrophobic interactions, facilitating the revelation of the domain-swapped structure. The negative cotton effect linked to the beta-sheet structure, observed around 215 nm in the circular dichroism (CD) spectrum of the tetrameric variable region, is more pronounced than that of the monomer. This suggests that the monomer contains less beta-sheet structures and exhibits greater flexibility than the tetramer in solution. These findings not only clarify the domain-swapped structure of the antibody light chain but also contribute to controlling antibody quality and advancing the development of future molecular recognition agents and drugs.

Structural and thermodynamic insights into antibody light chain tetramer formation through 3D domain swapping.,Sakai T, Mashima T, Kobayashi N, Ogata H, Duan L, Fujiki R, Hengphasatporn K, Uda T, Shigeta Y, Hifumi E, Hirota S Nat Commun. 2023 Dec 8;14(1):7807. doi: 10.1038/s41467-023-43443-4. PMID:38065949<ref>PMID:38065949</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 8kad" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Hifumi E]]
[[Category: Hirota S]]
[[Category: Kobayashi N]]
[[Category: Mashima T]]
[[Category: Ogata H]]
[[Category: Sakai T]]
[[Category: Uda T]]