A secondary C1s interaction site on C1‐inhibitor is essential for formation of a stable enzyme‐inhibitor complex

FEBS Letters

Sim, R.B²  He, Shiping¹  Whaley, K¹ 

[1] Department of Microbiology and Immunology, Medical Sciences Building, University of Leicester, University Road, Leicester LE1 9HN, UK;MRC Immunochemistry Unit, Department of Biochemistry, Oxford University, South Parks Road, Oxford OX1 3QU, UK

关键词: Human;    Autoantibody;    Complement;   

DOI  :  10.1016/S0014-5793(96)01529-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This paper examines the location of a secondary binding site for C1s on C1-inhibitor (C1-inh) which is required for the formation of SDS-stable C1s-C1-inh complexes. We used a synthetic peptide (residues 448–459) corresponding to the distal hinge region of C1-inh. This peptide binds to C1s and C1s preincubated with the peptide cleaves C1-inh but does not form a stable C1s-C1-inh complex. Computer modelling of C1-inh shows that residues Q452, Q453 and F455 are surface-exposed and that the secondary binding site may also include residues H291 and F292 which are conserved in serpins.© 1997 Federation of European Biochemical Societies.

【 授权许可】

Unknown