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The quaternary structure in solution of human complement subcomponent C1r2C1s2.

S J Perkins¹, A S Nealis

¹Department of Biochemistry and Chemistry, Royal Free Hospital School of Medicine, Hampstead, London, U.K.

The Biochemical Journal

|October 15, 1989

Summary

The structure of C1r2C1s2, a complement cascade component, was investigated. Hydrodynamic simulations and neutron scattering data support an X-shaped model over a linear one for C1r2 and C1r2C1s2.

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Area of Science:

Biochemistry
Molecular Biology
Immunology

Background:

The first component of the complement cascade (C1) comprises subcomponents including C1r and C1s.
Previous structural models for the C1r2C1s2 subcomponent proposed either a linear rod-like or an asymmetric X-shaped arrangement of globular domains.

Purpose of the Study:

To resolve the structural ambiguity of the C1r2C1s2 subcomponent.
To determine the arrangement of globular domains within C1r2C1s2 using biophysical methods.

Main Methods:

Hydrodynamic simulations
Neutron scattering analyses
Sedimentation coefficient measurements
Electron microscopy

Main Results:

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Hydrodynamic data supported linear cylinders for C1s and C1r monomers but not for C1r2 or C1r2C1s2.
The X-shaped model accurately predicted experimental sedimentation coefficients for C1r2 and C1r2C1s2.
Neutron scattering data were consistent with a linear structure for C1s but favored an X-shaped structure for C1r2.
The total length of C1s and C1r monomers was determined to be 17-20 nm.

Conclusions:

The experimental data strongly support an asymmetric X-shaped structure for C1r2 and C1r2C1s2.
The determined monomer length is consistent with the arrangement of known protein domains.