Structural basis for the growth factor activity of human adenosine deaminase ADA2

Journal of Biological Chemistry

Volumn 285, Issue 16, 2010, Pages 12367-12377

  Zavialov, Anton V ^a   Yu, Xiaodi ^a   Spillmann, Dorothe ^b   Lauvau, Grégoire ^c,d   Zavialo, Andrey V ^d,e  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b UPPSALA UNIVERSITY   (Sweden)

^c INSERM   (France)

^d ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^e AGENCY FOR SCIENCE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DEAMINASES; CATALYTIC DOMAINS; CATALYTIC SITES; CELL SURFACE RECEPTORS; COMPLEX ARCHITECTURES; DISULFIDE BONDS; EXTRACELLULAR ENVIRONMENTS; GROWTH FACTOR; IMMUNE SYSTEMS; NOVEL FOLDS; PATHOPHYSIOLOGICAL; PROTEIN DIMERIZATION; RATIONAL DESIGN; SEVERE COMBINED IMMUNODEFICIENCIES; SHARP CONTRAST; SIGNAL PEPTIDE; SINGLE DOMAINS; STRUCTURAL BASIS; STRUCTURAL DIFFERENCES; SUBSTRATE-BINDING; TISSUE DEVELOPMENT; TRANSITION-STATE ANALOGUES;

BIOACTIVITY; CELL MEMBRANES; CRYSTAL STRUCTURE; PEPTIDES;

BINDING SITES;

ADENOSINE DEAMINASE 1; ADENOSINE DEAMINASE 2; HYDROLASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN GLYCOSYLATION; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ADENOSINE DEAMINASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; COFORMYCIN; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; GROWTH SUBSTANCES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; STATIC ELECTRICITY; THERMODYNAMICS; TRANSCRIPTION FACTORS;

EID: 77951247730     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.083527     Document Type: Article

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