7b29

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Current revision (07:46, 1 May 2024) (edit) (undo)
 
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<StructureSection load='7b29' size='340' side='right'caption='[[7b29]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
<StructureSection load='7b29' size='340' side='right'caption='[[7b29]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7b29]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B29 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7b29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhipicephalus_appendiculatus Rhipicephalus appendiculatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B29 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7b26|7b26]], [[7b2d|7b2d]], [[7b28|7b28]], [[7b2a|7b2a]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=7b29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b29 OCA], [https://pdbe.org/7b29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b29 RCSB], [https://www.ebi.ac.uk/pdbsum/7b29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b29 ProSAT]</span></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=7b29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b29 OCA], [https://pdbe.org/7b29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b29 RCSB], [https://www.ebi.ac.uk/pdbsum/7b29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b29 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Activation of the serum-resident complement system begins a cascade that leads to activation of membrane-resident complement receptors on immune cells, thus coordinating serum and cellular immune responses. Whilst many molecules act to control inappropriate activation, Properdin is the only known positive regulator of the human complement system. By stabilising the alternative pathway C3 convertase it promotes complement self-amplification and persistent activation boosting the magnitude of the serum complement response by all triggers. In this work, we identify a family of tick-derived alternative pathway complement inhibitors, hereafter termed CirpA. Functional and structural characterisation reveals that members of the CirpA family directly bind to properdin, inhibiting its ability to promote complement activation, and leading to potent inhibition of the complement response in a species specific manner. We provide a full functional and structural characterisation of a properdin inhibitor, opening avenues for future therapeutic approaches.
 
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Structure and function of a family of tick-derived complement inhibitors targeting properdin.,Braunger K, Ahn J, Jore MM, Johnson S, Tang TTL, Pedersen DV, Andersen GR, Lea SM Nat Commun. 2022 Jan 14;13(1):317. doi: 10.1038/s41467-021-27920-2. PMID:35031611<ref>PMID:35031611</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 7b29" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Braunger, K]]
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[[Category: Rhipicephalus appendiculatus]]
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[[Category: Johnson, S]]
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[[Category: Braunger K]]
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[[Category: Lea, S M]]
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[[Category: Johnson S]]
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[[Category: Complement]]
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[[Category: Lea SM]]
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[[Category: Immunosuppressant]]
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[[Category: Inhibitor]]
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[[Category: Tick]]
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Current revision

Complement inhibitor CirpA4 from Rhipicephalus appendiculatus

PDB ID 7b29

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