The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex

EMBO Journal

Volumn 21, Issue 3, 2002, Pages 231-239

  Budayova Spano, Monika ^a   Lacroix, Monique ^a   Thielens, Nicole M ^a   Arlaud, Gérard J ^a   Fontecilla Camps, Juan Carlos ^a   Gaboriaud, Christine ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

Activation; Complement; Innate immunity; Modular structure; Serine protease

Indexed keywords

COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C2; ENZYME PRECURSOR; MONOMER; PROTEINASE; SERINE PROTEINASE;

ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; HUMAN; HUMAN CELL; IMMUNITY; MECHANICAL STRESS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CATALYSIS; COMPLEMENT C1; COMPLEMENT C1R; COMPLEMENT PATHWAY, CLASSICAL; ENZYME PRECURSORS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; STRESS, MECHANICAL; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0036469280     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/21.3.231     Document Type: Article

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