3zd1: Difference between revisions
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==STRUCTURE OF THE TWO C-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 2== | ==STRUCTURE OF THE TWO C-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 2== | ||
<StructureSection load='3zd1' size='340' side='right' caption='[[3zd1]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3zd1' size='340' side='right'caption='[[3zd1]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zd1]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3zd1]] 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=3ZD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZD1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zd1 OCA], [https://pdbe.org/3zd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zd1 RCSB], [https://www.ebi.ac.uk/pdbsum/3zd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zd1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/FHR2_HUMAN FHR2_HUMAN] Might be involved in complement regulation. Can associate with lipoproteins and may play a role in lipid metabolism. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3zd1" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Caesar JJE]] | ||
[[Category: | [[Category: Goicoechea de Jorge E]] | ||
[[Category: | [[Category: Lea SM]] | ||
[[Category: | [[Category: Pickering MC]] | ||
Latest revision as of 13:59, 20 December 2023
STRUCTURE OF THE TWO C-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 2STRUCTURE OF THE TWO C-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 2
Structural highlights
FunctionFHR2_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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