Cyclin B and cyclin A confer different substrate recognition properties on CDK2

Cell Cycle

Volumn 6, Issue 11, 2007, Pages 1350-1359

  Brown, Nick R ^a   Lowe, Ed D ^a   Petri, Ed ^b   Skamnaki, Vicky ^c   Antrobus, Robin ^a   Johnson, Louise N ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF ROCHESTER   (United States)

^c INSTITUTE OF BIOLOGY   (Greece)

Author keywords

CDK2; Cyclin B; Cyclin dependent protein kinase; Protein kinase structure; Substrate recognition

Indexed keywords

CYCLIN A; CYCLIN B; CYCLIN DEPENDENT KINASE 2; HEPTAPEPTIDE; LYSINE; CCNA2 PROTEIN, HUMAN; CDK2 PROTEIN, HUMAN; CYCLIN B1; CYCLIN DEPENDENT KINASE INHIBITOR 1B; HYBRID PROTEIN; LAMIN; PEPTIDE FRAGMENT; PROTEIN P107; RBL1 PROTEIN, HUMAN; UNCLASSIFIED DRUG;

ARTICLE; CARBONYLATION; CATALYSIS; CELL CYCLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ASSAY; ENZYME SPECIFICITY; HUMAN; HUMAN CELL; HYDROGEN BOND; INFORMATION PROCESSING; PHOSPHORYLATION; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; CELL CYCLE S PHASE; CELL DIVISION; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ELECTROSPRAY MASS SPECTROMETRY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; HYDROPHOBICITY; METABOLISM; MOLECULAR GENETICS; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN PROCESSING; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; SURFACE PLASMON RESONANCE; TANDEM MASS SPECTROMETRY; X RAY CRYSTALLOGRAPHY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CELL DIVISION; CRYSTALLOGRAPHY, X-RAY; CYCLIN A; CYCLIN B; CYCLIN-DEPENDENT KINASE 2; CYCLIN-DEPENDENT KINASE INHIBITOR P27; ENZYME ACTIVATION; HUMANS; HYDROPHOBICITY; LAMINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT FUSION PROTEINS; RETINOBLASTOMA-LIKE PROTEIN P107; S PHASE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; SURFACE PLASMON RESONANCE; TANDEM MASS SPECTROMETRY;

EID: 34547697834     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.6.11.4278     Document Type: Article

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