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2bzm
From Proteopedia
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[[Image:2bzm.gif|left|200px]] | [[Image:2bzm.gif|left|200px]] | ||
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'''SOLUTION STRUCTURE OF THE PRIMARY HOST RECOGNITION REGION OF COMPLEMENT FACTOR H''' | '''SOLUTION STRUCTURE OF THE PRIMARY HOST RECOGNITION REGION OF COMPLEMENT FACTOR H''' | ||
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[[Category: Pangburn, M K.]] | [[Category: Pangburn, M K.]] | ||
[[Category: Uhrin, D.]] | [[Category: Uhrin, D.]] | ||
| - | [[Category: | + | [[Category: Factor h,complement,hus,heparin,polyanions,immune response]] |
| - | [[Category: | + | [[Category: Innate immunity,complement alternate pathway,immune system]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:01:21 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:01, 3 May 2008
SOLUTION STRUCTURE OF THE PRIMARY HOST RECOGNITION REGION OF COMPLEMENT FACTOR H
Overview
Mutations and polymorphisms in the regulator of complement activation, factor H, have been linked to atypical hemolytic uremic syndrome (aHUS), membranoproliferative glomerulonephritis, and age-related macular degeneration. Many aHUS patients carry mutations in the two C-terminal modules of factor H, which normally confer upon this abundant 155-kDa plasma glycoprotein its ability to selectively bind self-surfaces and prevent them from inappropriately triggering the complement cascade via the alternative pathway. In the current study, the three-dimensional solution structure of the C-terminal module pair of factor H has been determined. A binding site for a fully sulfated heparin-derived tetrasaccharide has been delineated using chemical shift mapping and the C3d/C3b-binding site inferred from sequence comparisons and computational docking. The resultant information allows assessment of the likely consequences of aHUS-associated amino acid substitutions in this critical region of factor H. It is striking that, excepting those likely to perturb the three-dimensional structure, aHUS-associated missense mutations congregate in the polyanion-binding site delineated in this study, thus potentially disrupting a vital mechanism for control of complement on self-surfaces in the microvasculature of the kidney. It is intriguing that a single nucleotide polymorphism predisposing to age-related macular degeneration occupies another region of factor H that harbors a polyanion-binding site.
About this Structure
2BZM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure., Herbert AP, Uhrin D, Lyon M, Pangburn MK, Barlow PN, J Biol Chem. 2006 Jun 16;281(24):16512-20. Epub 2006 Mar 13. PMID:16533809 Page seeded by OCA on Sat May 3 21:01:21 2008
