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2qfh

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[[Image:2qfh.jpg|left|200px]]
[[Image:2qfh.jpg|left|200px]]
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{{Structure
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|PDB= 2qfh |SIZE=350|CAPTION= <scene name='initialview01'>2qfh</scene>
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The line below this paragraph, containing "STRUCTURE_2qfh", creates the "Structure Box" on the page.
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|GENE= CFH, HF, HF1, HF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2qfh| PDB=2qfh | SCENE= }}
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|RELATEDENTRY=[[1hcc|1HCC]], [[2g7i|2G7I]], [[1haq|1HAQ]], [[2qfg|2QFG]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qfh OCA], [http://www.ebi.ac.uk/pdbsum/2qfh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qfh RCSB]</span>
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'''Solution Structure of the C-terminal SCR-16/20 fragment of Complement Factor H.'''
'''Solution Structure of the C-terminal SCR-16/20 fragment of Complement Factor H.'''
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[[Category: Ormsby, R J.]]
[[Category: Ormsby, R J.]]
[[Category: Perkins, S J.]]
[[Category: Perkins, S J.]]
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[[Category: age-related macular degeneration]]
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[[Category: Age-related macular degeneration]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: complement]]
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[[Category: Complement]]
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[[Category: complement alternate pathway]]
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[[Category: Complement alternate pathway]]
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[[Category: disease mutation]]
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[[Category: Disease mutation]]
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[[Category: factor h]]
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[[Category: Factor h]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: immune response]]
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[[Category: Immune response]]
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[[Category: immune system]]
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[[Category: Immune system]]
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[[Category: innate immunity]]
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[[Category: Innate immunity]]
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[[Category: polymorphism]]
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[[Category: Polymorphism]]
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[[Category: scr domain]]
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[[Category: Scr domain]]
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[[Category: sushi]]
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[[Category: Sushi]]
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[[Category: x-ray scattering]]
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[[Category: X-ray scattering]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:52:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:48:44 2008''
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Revision as of 11:52, 4 May 2008

Image:2qfh.jpg

Template:STRUCTURE 2qfh

Solution Structure of the C-terminal SCR-16/20 fragment of Complement Factor H.


Overview

Factor H (FH) is a plasma glycoprotein that plays a central role in regulation of the alternative pathway of complement. It is composed of 20 short complement regulator (SCR) domains. The SCR-1/5 fragment is required for decay acceleration and cofactor activity, while the SCR-16/20 fragment possesses binding sites for complement C3d and heparin. X-ray scattering and analytical ultracentrifugation showed that SCR-1/5 was monomeric, while SCR-16/20 formed dimers. The Guinier radius of gyration R(G) of 4.3 nm for SCR-1/5 and those of 4.7 nm and about 7.8 nm for monomeric and dimeric SCR-16/20, respectively, showed that their structures are partially folded back and bent. The distance distribution function P(r) showed that SCR-1/5 has a maximum dimension of 15 nm while monomeric and dimeric SCR-16/20 are 17 nm and about 27 nm long, respectively. The sedimentation coefficient of 2.4 S for SCR-1/5 showed no concentration-dependence, while that for SCR-16/20 was 2.8 S for the monomer and 3.9 S for the dimer. Sedimentation equilibrium data showed that SCR-1/5 is monomeric while SCR-16/20 exhibited a weak monomer-dimer equilibrium with a dissociation constant of 16 microM. The constrained scattering and sedimentation modelling of SCR-1/5 and SCR-16/20 showed that partially folded-back and bent flexible SCR arrangements fitted both data sets better than extended linear arrangements, and that the dimer was best modelled in the SCR-16/20 model by an end-to-end association of two SCR-20 domains. The SCR-1/5 and SCR-16/20 models were conformationally similar to the previously determined partially folded-back structure for intact wild-type FH, hence suggesting a partial explanation of the intact FH structure. Comparison of the SCR-16/20 model with the crystal structure of C3b clarified reasons for the distribution of mutations leading to atypical haemolytic uraemic syndrome.

About this Structure

2QFH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties., Okemefuna AI, Gilbert HE, Griggs KM, Ormsby RJ, Gordon DL, Perkins SJ, J Mol Biol. 2008 Jan 4;375(1):80-101. Epub 2007 Sep 14. PMID:18005991 Page seeded by OCA on Sun May 4 14:52:29 2008

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