Molecular modeling of human complement component C4 and its fragments by x-ray and neutron solution scattering

Biochemistry ◽  
1990 ◽  
Vol 29 (5) ◽  
pp. 1167-1175 ◽  
Author(s):  
Stephen J. Perkins ◽  
Adam S. Nealis ◽  
Robert B. Sim
1986 ◽  
Vol 233 (3) ◽  
pp. 799-807 ◽  
Author(s):  
S J Perkins ◽  
L P Chung ◽  
K B M Reid

Solution X-ray-scattering experiments with the use of synchrotron radiation on the human complement-component-C4b-binding protein showed that its RG is 13 nm and that its Mr is 550,000. From the known primary amino acid sequence and estimated carbohydrate content, C4b-binding protein is inferred to have a total of 7.4 +/- 1 subunits. Heptameric computer models for C4b-binding protein were based on the X-ray-scattering curve to a resolution of 6.4 nm, and literature values for sedimentation coefficients and electron-microscopy images. The macromolecule was represented by a bundle of seven arms held together at the C-terminal end and spaced out by a base containing 23% of C4b-binding protein by volume. If the overall length of each arm is assumed to be 33 nm as seen in electron microscopy, the solution data indicate an average arm-axis angle of 5-10 degrees. The seven arms of C4b-binding protein are found to be close together, in distinction to the splayed-out images seen in electron micrographs.


2002 ◽  
Vol 322 (5) ◽  
pp. 1103-1115 ◽  
Author(s):  
Jean M.H. van den Elsen ◽  
Alberto Martin ◽  
Veronica Wong ◽  
Liliana Clemenza ◽  
David R. Rose ◽  
...  

1988 ◽  
Vol 263 (1) ◽  
pp. 549-560
Author(s):  
R G DiScipio ◽  
D N Chakravarti ◽  
H J Muller-Eberhard ◽  
G H Fey

1987 ◽  
Vol 15 (5) ◽  
pp. 2395-2395 ◽  
Author(s):  
A. Palsdottir ◽  
R. Fossdal ◽  
O. Jensson ◽  
A. Amason

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