Tandem Domains with Tuned Interactions Are a Powerful Biological Design Principle

PLoS Biology

Volumn 13, Issue 11, 2015, Pages

  Nussinov, Ruth ^a,b,c   Tsai, Chung Jung ^a,b  

^a FREDERICK NATIONAL LABORATORY FOR CANCER RESEARCH   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

^c TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE REGULATORY SUBUNIT IALPHA; CYCLIC AMP DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT; ENZYME; LIGAND; PROTEIN SUBUNIT;

BINDING AFFINITY; BINDING SITE; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; LIGAND BINDING; MOLECULAR RECOGNITION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN PROCESSING; PROTEIN STABILITY; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION; ANIMAL; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR MODEL; MUTATION; PROTEIN CONFORMATION; PROTEIN SUBUNIT; TANDEM REPEAT;

ANIMALS; CYCLIC AMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNITS; CYCLIC AMP-DEPENDENT PROTEIN KINASE RIALPHA SUBUNIT; ENZYME ACTIVATION; ENZYMES; EVOLUTION, MOLECULAR; HUMANS; LIGANDS; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN SUBUNITS; TANDEM REPEAT SEQUENCES;

EID: 84949460582     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1002306     Document Type: Review

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