8uh2: Difference between revisions
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==Complex of C3b with the inhibitor albicin== | |||
<StructureSection load='8uh2' size='340' side='right'caption='[[8uh2]], [[Resolution|resolution]] 3.59Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8uh2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] 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=8UH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UH2 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]] 3.59Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=8uh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8uh2 OCA], [https://pdbe.org/8uh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8uh2 RCSB], [https://www.ebi.ac.uk/pdbsum/8uh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8uh2 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Salivary complement inhibitors occur in many of the blood feeding arthropod species responsible for transmission of pathogens. During feeding, these inhibitors prevent the production of proinflammatory anaphylatoxins, which may interfere with feeding, and limit formation of the membrane attack complex which could damage arthropod gut tissues. Salivary inhibitors are, in many cases, novel proteins which may be pharmaceutically useful or display unusual mechanisms that could be exploited pharmaceutically. Albicin is a potent inhibitor of the alternative pathway of complement from the saliva of the malaria transmitting mosquito, Anopheles albimanus. Here we describe the cryo-EM structure of albicin bound to C3bBb, the alternative C3 convertase, a proteolytic complex that is responsible for cleavage of C3 and amplification of the complement response. Albicin is shown to induce dimerization of C3bBb, in a manner similar to the bacterial inhibitor SCIN, to form an inactive complex unable to bind the substrate C3. Size exclusion chromatography and structures determined after 30 minutes of incubation of C3b, factor B (FB), factor D (FD) and albicin indicate that FBb dissociates from the inhibited dimeric complex leaving a C3b-albicin dimeric complex which apparently decays more slowly. | |||
Mechanism of complement inhibition by a mosquito protein revealed through cryo-EM.,Andersen JF, Lei H, Strayer EC, Pham V, Ribeiro JMC Commun Biol. 2024 May 27;7(1):649. doi: 10.1038/s42003-024-06351-x. PMID:38802531<ref>PMID:38802531</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Andersen | <div class="pdbe-citations 8uh2" style="background-color:#fffaf0;"></div> | ||
[[Category: Lei | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Anopheles albimanus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Andersen JF]] | |||
[[Category: Lei H]] | |||
[[Category: Ribeiro JM]] | |||
[[Category: Strayer E]] | |||
Latest revision as of 10:43, 21 November 2024
Complex of C3b with the inhibitor albicinComplex of C3b with the inhibitor albicin
Structural highlights
Publication Abstract from PubMedSalivary complement inhibitors occur in many of the blood feeding arthropod species responsible for transmission of pathogens. During feeding, these inhibitors prevent the production of proinflammatory anaphylatoxins, which may interfere with feeding, and limit formation of the membrane attack complex which could damage arthropod gut tissues. Salivary inhibitors are, in many cases, novel proteins which may be pharmaceutically useful or display unusual mechanisms that could be exploited pharmaceutically. Albicin is a potent inhibitor of the alternative pathway of complement from the saliva of the malaria transmitting mosquito, Anopheles albimanus. Here we describe the cryo-EM structure of albicin bound to C3bBb, the alternative C3 convertase, a proteolytic complex that is responsible for cleavage of C3 and amplification of the complement response. Albicin is shown to induce dimerization of C3bBb, in a manner similar to the bacterial inhibitor SCIN, to form an inactive complex unable to bind the substrate C3. Size exclusion chromatography and structures determined after 30 minutes of incubation of C3b, factor B (FB), factor D (FD) and albicin indicate that FBb dissociates from the inhibited dimeric complex leaving a C3b-albicin dimeric complex which apparently decays more slowly. Mechanism of complement inhibition by a mosquito protein revealed through cryo-EM.,Andersen JF, Lei H, Strayer EC, Pham V, Ribeiro JMC Commun Biol. 2024 May 27;7(1):649. doi: 10.1038/s42003-024-06351-x. PMID:38802531[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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