Neutron scattering study of the (γ‐B) catalytic domains of complement proteases Cl̄r and Cl̄s

FEBS Letters

Zaccaï, Giuseppe²  Thielens, Nicole M.¹  Aude, Catherine A.¹  Arlaud, Gérard J.¹ 

[1] Unité INSERM 238, Département de Recherche Fondamentale. Laboratoire d'Immunochimie, Centre d'Etudes Nucléaires de Grenoble, 85X, 38041 Grenoble Cedex, France;NRS URA 1333, Institut Laue Langevin, 156X, 38042 Grenoble Cedex, France

关键词: Complement system;    Serine protease;    Clr;    CIs;    Protein domain;    Neutron scattering;    The nomenclature of complement components is that recommended by the World Health Organization;    activated components are indicated by a superscript bar;    e.g. Cl̄r. iPr2P-F;    diisopropylphosphorofluoridate;   

DOI  :  10.1016/0014-5793(90)81108-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The catalytic domains of Cl̄r and Cl̄s, comprising the C-tenninal region of the A chain (γ), disulphide-linked to the B chain, were obtained by limited proteolysis of the native proteases with chymotrypsin and plasmin, respectively, and studied by small angle neutron scattering. For CIs (γ-B), a molar mass of 45 000 ± 5000 , and a relatively large radius of gyration (R _g) of 28 ± 1 Å were determined, excluding a single globular domain. The corresponding values for Cl̄r (γ-B), (90,000 , R _g, = 34 ± 1 Å) are consistent with a dimer involving the loose packing of two (γ-B) subunits. Various models of the dimer are discussed in the light of neutron scattering and other data.

【 授权许可】

Unknown