5h8d: Difference between revisions
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==Crystal structure of an ASC binding nanobody== | ==Crystal structure of an ASC binding nanobody== | ||
<StructureSection load='5h8d' size='340' side='right' caption='[[5h8d]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='5h8d' size='340' side='right'caption='[[5h8d]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5h8d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H8D OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5h8d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H8D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H8D FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h8o|5h8o]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h8o|5h8o]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h8d OCA], [http://pdbe.org/5h8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h8d RCSB], [http://www.ebi.ac.uk/pdbsum/5h8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h8d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5h8d" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5h8d" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Camelus glama]] | |||
[[Category: Large Structures]] | |||
[[Category: Lu, A]] | [[Category: Lu, A]] | ||
[[Category: Ploegh, H L]] | [[Category: Ploegh, H L]] | ||
Revision as of 09:55, 20 May 2020
Crystal structure of an ASC binding nanobodyCrystal structure of an ASC binding nanobody
Structural highlights
Publication Abstract from PubMedMyeloid cells assemble inflammasomes in response to infection or cell damage; cytosolic sensors activate pro-caspase-1, indirectly for the most part, via the adaptors ASC and NLRC4. This leads to secretion of proinflammatory cytokines and pyroptosis. To explore complex formation under physiological conditions, we generated an alpaca single domain antibody, VHHASC, which specifically recognizes the CARD of human ASC via its type II interface. VHHASC not only impairs ASC(CARD) interactions in vitro, but also inhibits inflammasome activation in response to NLRP3, AIM2, and NAIP triggers when expressed in living cells, highlighting a role of ASC in all three types of inflammasomes. VHHASC leaves the Pyrin domain of ASC functional and stabilizes a filamentous intermediate of inflammasome activation. Incorporation of VHHASC-EGFP into these structures allowed the visualization of endogenous ASC(PYD) filaments for the first time. These data revealed that cross-linking of ASC(PYD) filaments via ASC(CARD) mediates the assembly of ASC foci. A single domain antibody fragment that recognizes the adaptor ASC defines the role of ASC domains in inflammasome assembly.,Schmidt FI, Lu A, Chen JW, Ruan J, Tang C, Wu H, Ploegh HL J Exp Med. 2016 May 2;213(5):771-90. doi: 10.1084/jem.20151790. Epub 2016 Apr 11. PMID:27069117[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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