Structural basis of profactor D activation: From a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D

EMBO Journal

Volumn 18, Issue 4, 1999, Pages 804-814

  Jing, Hua ^a   Macon, Kevin J ^b   Moore, Dwight ^a   DeLucas, Lawrence J ^a   Volanakis, John E ^b,c   Narayana, Sthanam V L ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b The University of Alabama at Birmingham   (United States)

^c BIOMEDICAL SCIENCES RESEARCH CENTER ALEXANDER FLEMING   (Greece)

Author keywords

Conformational change; Crystal structure; Factor D; Serine protease; Zymogen activation

Indexed keywords

ARGININE; ASPARTIC ACID; CHYMOTRYPSINOGEN; COMPLEMENT FACTOR D; ENZYME PRECURSOR; ISOLEUCINE; LEUCINE; SERINE PROTEINASE; TRYPSINOGEN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; R FACTOR;

AMINO ACID SEQUENCE; BINDING SITES; COMPLEMENT FACTOR D; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ENZYME PRECURSORS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN PRECURSORS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES;

STAPHYLOCOCCUS PHAGE 187;

EID: 0033557766     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.4.804     Document Type: Article

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