2qfh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2qfh.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2qfh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qfh| PDB=2qfh | SCENE= }}
{{STRUCTURE_2qfh| PDB=2qfh | SCENE= }}
-
'''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.===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18005991}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18005991 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18005991}}
==About this Structure==
==About this Structure==
Line 42: Line 46:
[[Category: Sushi]]
[[Category: Sushi]]
[[Category: X-ray scattering]]
[[Category: X-ray scattering]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:52:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:37:36 2008''

Revision as of 23:37, 27 July 2008

Image:2qfh.png

Template:STRUCTURE 2qfh

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

Template:ABSTRACT PUBMED 18005991

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 Mon Jul 28 02:37:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qfh"
Personal tools