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(New page: 200px<br /> <applet load="2qfg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2qfg" /> '''Solution Structure of the N-terminal SCR-1/...) |
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'''Solution Structure of the N-terminal SCR-1/5 fragment of Complement Factor H.'''<br /> | '''Solution Structure of the N-terminal SCR-1/5 fragment of Complement Factor H.'''<br /> | ||
| - | == | + | ==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== | ==About this Structure== | ||
| - | 2QFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2QFG is a [http://en.wikipedia.org/wiki/Single_protein 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=2QFG 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18005991 18005991] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 32: | Line 34: | ||
[[Category: x-ray scattering]] | [[Category: x-ray scattering]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:31:33 2008'' |
Revision as of 09:31, 23 January 2008
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Solution Structure of the N-terminal SCR-1/5 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
2QFG 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 Wed Jan 23 11:31:33 2008
Categories: Homo sapiens | Single protein | Gilbert, H.E. | Gordon, D.L. | Griggs, K.M. | Okemefuna, A.I. | Ormsby, R.J. | Perkins, S.J. | Age-related macular degeneration | Alternative splicing | Complement | Complement alternate pathway | Disease mutation | Factor h | Glycoprotein | Immune response | Immune system | Innate immunity | Polymorphism | Scr domain | Sushi | X-ray scattering
