Hydrodynamic data show that C1̄ inhibitor of complement forms compact complexes with C1̄r and C1̄s

FEBS Letters

Perkins, Stephen J.¹ 

[1] Departments of Biochemistry and Chemistry, and of Protein and Molecular Biology, Royal Free Hospital School of Medicine, Rowland Hill St., London NW3 2PF, UK

关键词: C1̄ inhibitor;    Clr;    Cls;    Complement;    Sedimentation coefficient;    Hydrodynamic simulation;   

DOI  :  10.1016/0014-5793(90)80379-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The C1̄ inhibitor of the complement cascade forms stoichiometric complexes with C1̄r and C1̄s and controls the activation of first component C1 of complement. Literature sedimentation coefficients s°_20.w for the complexes formed between C1̄ inhibitor, C1̄r and C1̄s were analysed using frictional ratios and the hydrodynamic sphere approach. A head-and-tail two-domain model for C1 inhibitor was combined with cylindrical hydrodynamic models for the six-domain structures of C1̄r and C1̄s. The hydrodynamic data show that the heavily glycosylated N-terminal domain of C1̄ inhibitor is positioned close to the two complement ‘short consensus repeat’ domains found in the centre of C1̄r and C1̄s.

【 授权许可】

Unknown