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The C4b-Binding Protein Protein S Interaction Is Hydrophobic in Nature

  1. Author:
    Blom, A. M.
    Covell, D. G.
    Wallqvist, A.
    Dahlback, B.
    Villoutreix, B. O.

  2. Author Address

    Villoutreix BO LUND UNIV MALMO UNIV HOSP DEPT CLIN CHEM WALLENBERG LAB S-20502 MALMO SWEDEN LUND UNIV MALMO UNIV HOSP DEPT CLIN CHEM WALLENBERG LAB S-20502 MALMO SWEDEN NCI FREDERICK CANC RES & DEV CTR SCI APPLICAT INT CORP FREDERICK, MD 21702 USA RUTGERS STATE UNIV DEPT CHEM PISCATAWAY, NJ 08855 USA
    1. Year: 1998
  2. Journal: Biochimica et Biophysica Acta - Protein Structure & Molecular Enzymology
    1. 1388
    2. 1
    3. Pages: 181-189
  4. Type of Article: Article
  1. Abstract:

    C4b-binding protein (C4BP) is a major regulatory molecule of the complement system. By forming a non covalent complex with the anticoagulant cofactor protein S (PS), it also plays an important role in blood coagulation. C4BP is composed of one beta-chain and seven alpha-chains that are essentially built from complement control protein (CCP)-modules. Our group has previously reported that the first (N-terminal) CCP module of the beta-chain (beta CCP1) contains the entire binding site for protein S, We now investigate further the binding of protein S to C4BP and show that the complex formation is essentially dependent on hydrophobic forces with minor contribution from electrostatic interactions. This result is in agreement with homology modeling experiments carried out in conjunction with inter-species sequence comparison and theoretical enumeration of potential binding sites. These methods pinpoint a solvent exposed hydrophobic cluster at the surface of the beta CCP1 module that is of crucial importance for the binding process. (C) 1998 Elsevier Science B.V. All rights reserved. [References: 30]

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