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''' | + | {{Structure |
| + | |PDB= 2bzm |SIZE=350|CAPTION= <scene name='initialview01'>2bzm</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF THE PRIMARY HOST RECOGNITION REGION OF COMPLEMENT FACTOR H''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BZM is a [ | + | 2BZM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16533809 16533809] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: immune system]] | [[Category: immune system]] | ||
[[Category: innate immunity]] | [[Category: innate immunity]] | ||
| - | [[Category: | + | [[Category: polyanion]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:08:52 2008'' |
Revision as of 14:08, 20 March 2008
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SOLUTION STRUCTURE OF THE PRIMARY HOST RECOGNITION REGION OF COMPLEMENT FACTOR H
Contents |
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.
Disease
Known diseases associated with this structure: Complement factor H deficiency OMIM:[134370], Factor H and factor H-like 1 OMIM:[134370], Hemolytic-uremic syndrome OMIM:[134370], Macular degeneration, age-related, 4 OMIM:[134370], Membranoproliferative glomerulonephritis with CFH deficiency OMIM:[134370]
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
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