3zd2: Difference between revisions
New page: '''Unreleased structure''' The entry 3zd2 is ON HOLD Authors: Caesar, J.J.E., Goicoechea de Jorge, E., Pickering, M.C., Lea, S.M. Description: THE STRUCTURE OF THE TWO N-TERMINAL DOMAI... |
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The | ==THE STRUCTURE OF THE TWO N-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 1 SHOWS FORMATION OF A NOVEL DIMERISATION INTERFACE== | ||
<StructureSection load='3zd2' size='340' side='right'caption='[[3zd2]], [[Resolution|resolution]] 1.99Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zd2]] is a 2 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=3ZD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZD2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=3zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zd2 OCA], [https://pdbe.org/3zd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zd2 RCSB], [https://www.ebi.ac.uk/pdbsum/3zd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zd2 ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/FHR1_HUMAN FHR1_HUMAN] Atypical hemolytic uremic syndrome with antibody anti-factor H. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FHR1_HUMAN FHR1_HUMAN] Might be involved in complement regulation. Can associate with lipoproteins and may play a role in lipid metabolism. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The complement system is a key component regulation influences susceptibility to age-related macular degeneration, meningitis, and kidney disease. Variation includes genomic rearrangements within the complement factor H-related (CFHR) locus. Elucidating the mechanism underlying these associations has been hindered by the lack of understanding of the biological role of CFHR proteins. Here we present unique structural data demonstrating that three of the CFHR proteins contain a shared dimerization motif and that this hitherto unrecognized structural property enables formation of both homodimers and heterodimers. Dimerization confers avidity for tissue-bound complement fragments and enables these proteins to efficiently compete with the physiological complement inhibitor, complement factor H (CFH), for ligand binding. Our data demonstrate that these CFHR proteins function as competitive antagonists of CFH to modulate complement activation in vivo and explain why variation in the CFHRs predisposes to disease. | |||
Dimerization of complement factor H-related proteins modulates complement activation in vivo.,Goicoechea de Jorge E, Caesar JJ, Malik TH, Patel M, Colledge M, Johnson S, Hakobyan S, Morgan BP, Harris CL, Pickering MC, Lea SM Proc Natl Acad Sci U S A. 2013 Mar 19;110(12):4685-90. doi:, 10.1073/pnas.1219260110. Epub 2013 Mar 4. PMID:23487775<ref>PMID:23487775</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zd2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Caesar JJE]] | |||
[[Category: Goicoechea de Jorge E]] | |||
[[Category: Lea SM]] | |||
[[Category: Pickering MC]] | |||
Latest revision as of 13:59, 20 December 2023
THE STRUCTURE OF THE TWO N-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 1 SHOWS FORMATION OF A NOVEL DIMERISATION INTERFACETHE STRUCTURE OF THE TWO N-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 1 SHOWS FORMATION OF A NOVEL DIMERISATION INTERFACE
Structural highlights
DiseaseFHR1_HUMAN Atypical hemolytic uremic syndrome with antibody anti-factor H. FunctionFHR1_HUMAN Might be involved in complement regulation. Can associate with lipoproteins and may play a role in lipid metabolism. Publication Abstract from PubMedThe complement system is a key component regulation influences susceptibility to age-related macular degeneration, meningitis, and kidney disease. Variation includes genomic rearrangements within the complement factor H-related (CFHR) locus. Elucidating the mechanism underlying these associations has been hindered by the lack of understanding of the biological role of CFHR proteins. Here we present unique structural data demonstrating that three of the CFHR proteins contain a shared dimerization motif and that this hitherto unrecognized structural property enables formation of both homodimers and heterodimers. Dimerization confers avidity for tissue-bound complement fragments and enables these proteins to efficiently compete with the physiological complement inhibitor, complement factor H (CFH), for ligand binding. Our data demonstrate that these CFHR proteins function as competitive antagonists of CFH to modulate complement activation in vivo and explain why variation in the CFHRs predisposes to disease. Dimerization of complement factor H-related proteins modulates complement activation in vivo.,Goicoechea de Jorge E, Caesar JJ, Malik TH, Patel M, Colledge M, Johnson S, Hakobyan S, Morgan BP, Harris CL, Pickering MC, Lea SM Proc Natl Acad Sci U S A. 2013 Mar 19;110(12):4685-90. doi:, 10.1073/pnas.1219260110. Epub 2013 Mar 4. PMID:23487775[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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