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Structural biology of C1: dissection of a complex molecular machinery
Author(s) -
Arlaud Gérard J.,
Gaboriaud Christine,
Thielens Nicole M.,
Rossi Véronique,
Bersch Beate,
Hernandez JeanFrançois,
FontecillaCamps Juan C.
Publication year - 2001
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1034/j.1600-065x.2001.1800112.x
Subject(s) - biology , tetramer , computational biology , modular design , proteases , structural biology , protein subunit , protein structure , function (biology) , modularity (biology) , structure function , serine protease , protease , microbiology and biotechnology , genetics , biochemistry , computer science , gene , enzyme , physics , particle physics , operating system
Summary: The classical pathway of complement is initiated by the C1 complex, a multimolecular protease comprising a recognition subunit (C1q) and two modular serine proteases (C1r and C1s) associated as a Ca 2+ ‐dependent tetramer (C1s‐C1r‐C1r‐C1s). Early studies have allowed identification of specialized functional domains in these proteins and have led to low‐resolution models of the C1 complex. The objective of current studies is to gain deeper insights into the structure of C1, and the strategy used for this purpose mainly consists of dissecting the C1 components into modular fragments, in order to solve their three‐dimensional structure and establish the structural correlates of their function. The aim of this article is to provide an overview of the structural and functional information generated by this approach, with particular emphasis on the domains involved in the assembly, the recognition function, and the highly specific proteolytic properties of C1. The original work cited in this review was supported in part by the Commissariat à l’Energie Atomique (CEA), the Centre National de la Recherche Scientifique, and the European Union Biotechnology programme.