Abstract:
:C1r, the enzyme responsible for intrinsic activation of the C1 complex of complement, is a modular serine protease featuring an overall structural organization homologous to those of C1s and the mannan-binding lectin-associated serine proteases (MASPs). This review will initially summarize current information on the structure and function of C1r, with particular emphasis on the three-dimensional structure of its catalytic domain, which provides new insights into the activation mechanism of C1. The second part of this review will focus on recent discoveries dealing with a truncated, C1r-related protein, and the occurrence in the mouse of two isoforms, C1rA and C1rB, exhibiting tissue-specific expression patterns.
journal_name
Immunobiologyjournal_title
Immunobiologyauthors
Arlaud GJ,Gaboriaud C,Garnier G,Circolo A,Thielens NM,Budayova-Spano M,Fontecilla-Camps JC,Volanakis JEdoi
10.1078/0171-2985-00139subject
Has Abstractpub_date
2002-09-01 00:00:00pages
365-82issue
4-5eissn
0171-2985issn
1878-3279pii
S0171-2985(04)70088-1journal_volume
205pub_type
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