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2bzm

From Proteopedia

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[[Image:2bzm.gif|left|200px]]
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{{Seed}}
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[[Image:2bzm.png|left|200px]]
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{{STRUCTURE_2bzm| PDB=2bzm | SCENE= }}
{{STRUCTURE_2bzm| PDB=2bzm | SCENE= }}
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'''SOLUTION STRUCTURE OF THE PRIMARY HOST RECOGNITION REGION OF COMPLEMENT FACTOR H'''
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===SOLUTION STRUCTURE OF THE PRIMARY HOST RECOGNITION REGION OF COMPLEMENT FACTOR H===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16533809}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16533809 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16533809}}
==About this Structure==
==About this Structure==
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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].
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2BZM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZM OCA].
==Reference==
==Reference==
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[[Category: Factor h,complement,hus,heparin,polyanions,immune response]]
[[Category: Factor h,complement,hus,heparin,polyanions,immune response]]
[[Category: Innate immunity,complement alternate pathway,immune system]]
[[Category: Innate immunity,complement alternate pathway,immune system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:01:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:00:34 2008''

Revision as of 12:00, 28 July 2008

Image:2bzm.png

Template:STRUCTURE 2bzm

SOLUTION STRUCTURE OF THE PRIMARY HOST RECOGNITION REGION OF COMPLEMENT FACTOR H

Template:ABSTRACT PUBMED 16533809

About this Structure

2BZM is a Single protein structure of sequence from Homo sapiens. Full experimental 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 Mon Jul 28 15:00:34 2008

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