9c9l
From Proteopedia
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(New page: '''Unreleased structure''' The entry 9c9l is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the C1q A, B-crt, C peptide assembly narrow region== | |
| - | + | <StructureSection load='9c9l' size='340' side='right'caption='[[9c9l]], [[Resolution|resolution]] 3.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9c9l]] is a 18 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=9C9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9C9L 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]] 3.7Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</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=9c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9c9l OCA], [https://pdbe.org/9c9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9c9l RCSB], [https://www.ebi.ac.uk/pdbsum/9c9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9c9l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/C1QB_HUMAN C1QB_HUMAN] Defects in C1QB are a cause of complement component C1q deficiency (C1QD) [MIM:[https://omim.org/entry/613652 613652]. A rare defect resulting in C1 deficiency and impaired activation of the complement classical pathway. C1 deficiency generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis.<ref>PMID:9476130</ref> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C1QB_HUMAN C1QB_HUMAN] C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes. | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Egelman EH]] | ||
| + | [[Category: Hartgerink JD]] | ||
| + | [[Category: Kreutzberger MA]] | ||
| + | [[Category: Yu LT]] | ||
Current revision
Cryo-EM structure of the C1q A, B-crt, C peptide assembly narrow region
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