3zd2

THE STRUCTURE OF THE TWO N-TERMINAL DOMAINS OF COMPLEMENT FACTOR H RELATED PROTEIN 1 SHOWS FORMATION OF A NOVEL DIMERISATION INTERFACE

spinqualitylabelsall models 3zd2, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zd2 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.99Å Ligands: EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease FHR1_HUMAN Atypical hemolytic uremic syndrome with antibody anti-factor H. Function FHR1_HUMAN Might be involved in complement regulation. Can associate with lipoproteins and may play a role in lipid metabolism. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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