8hlb: Difference between revisions

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-'''Unreleased structure'''
-The entry 8hlb is ON HOLD  until Paper Publication
+==Cryo-EM structure of biparatopic antibody Bp109-92 in complex with TNFR2==
+<StructureSection load='8hlb' size='340' side='right'caption='[[8hlb]], [[Resolution|resolution]] 3.63&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8hlb]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HLB FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.63&#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=8hlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hlb OCA], [https://pdbe.org/8hlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hlb RCSB], [https://www.ebi.ac.uk/pdbsum/8hlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hlb ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Conventional bivalent antibodies against cell surface receptors often initiate unwanted signal transduction by crosslinking two antigen molecules. Biparatopic antibodies (BpAbs) bind to two different epitopes on the same antigen, thus altering crosslinking ability. In this study, we develop BpAbs against tumor necrosis factor receptor 2 (TNFR2), which is an attractive immune checkpoint target. Using different pairs of antibody variable regions specific to topographically distinct TNFR2 epitopes, we successfully regulate the size of BpAb-TNFR2 immunocomplexes to result in controlled agonistic activities. Our series of results indicate that the relative positions of the two epitopes recognized by the BpAb are critical for controlling its signaling activity. One particular antagonist, Bp109-92, binds TNFR2 in a 1:1 manner without unwanted signal transduction, and its structural basis is determined using cryo-electron microscopy. This antagonist suppresses the proliferation of regulatory T cells expressing TNFR2. Therefore, the BpAb format would be useful in designing specific and distinct antibody functions.
-Authors:
+Development of a 1:1-binding biparatopic anti-TNFR2 antagonist by reducing signaling activity through epitope selection.,Akiba H, Fujita J, Ise T, Nishiyama K, Miyata T, Kato T, Namba K, Ohno H, Kamada H, Nagata S, Tsumoto K Commun Biol. 2023 Sep 27;6(1):987. doi: 10.1038/s42003-023-05326-8. PMID:37758868<ref>PMID:37758868</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8hlb" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Akiba H]]
+[[Category: Fujita J]]
+[[Category: Ise T]]
+[[Category: Kamada H]]
+[[Category: Kato T]]
+[[Category: Miyata T]]
+[[Category: Nagata S]]
+[[Category: Namba K]]
+[[Category: Nishiyama K]]
+[[Category: Ohno H]]
+[[Category: Tsumoto K]]