Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex

Journal of Biological Chemistry

Volumn 285, Issue 42, 2010, Pages 32251-32263

  Brier, Sébastien ^a   Pflieger, Delphine ^a   Le Mignon, Maxime ^a   Bally, Isabelle ^b   Gaboriaud, Christine ^b   Arlaud, Gérard J ^b   Daniel, Régis ^a  

^a UNIVERSITÉ D EVRY VAL D ESSONNE   (France)

^b UNIV GRENOBLE ALPES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

EXPERIMENTAL EVIDENCE; INTERACTION DOMAIN; LABEL FREE; LYSINE RESIDUES; PROTEIN SAMPLES; SEMI-QUANTITATIVE ANALYSIS; SERINE PROTEASE; SITE DIRECTED MUTAGENESIS; STRUCTURAL INSIGHTS; STRUCTURAL INVESTIGATION; TETRAMERS; THREE-DIMENSIONAL MODEL;

AMINO ACIDS; BINDING ENERGY; BIOCHEMISTRY; CHEMICAL MODIFICATION; ENZYME ACTIVITY; MASS SPECTROMETRY; THREE DIMENSIONAL;

BINDING SITES;

COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; ENZYME PRECURSOR; EPIDERMAL GROWTH FACTOR; LYSINE; PROCOLLAGEN C PROTEINASE; SERINE PROTEINASE; TETRAMER;

ACETYLATION; AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEMENT CLASSICAL PATHWAY; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVE SITE; HUMAN; LIQUID CHROMATOGRAPHY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN HYDROLYSIS; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; QUANTITATIVE ANALYSIS; STRUCTURE ANALYSIS; SURFACE PROPERTY;

AMINO ACID SEQUENCE; BINDING SITES; COMPLEMENT ACTIVATION; COMPLEMENT C1; COMPLEMENT C1R; COMPLEMENT C1S; HUMANS; LYSINE; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; STAINING AND LABELING; SURFACE PROPERTIES;

EID: 77957789299     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.149112     Document Type: Article

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