Molecular Architecture of SF3b and Structural Consequences of Its Cancer-Related Mutations

Molecular Cell

Volumn 64, Issue 2, 2016, Pages 307-319

  Cretu, Constantin ^a   Schmitzová, Jana ^a   Ponce Salvatierra, Almudena ^a   Dybkov, Olexandr ^a   De Laurentiis, Evelina I ^a   Sharma, Kundan ^a,b   Will, Cindy L ^a   Urlaub, Henning ^a,b   Lührmann, Reinhard ^a   Pena, Vladimir ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b UNIVERSITY MEDICAL CENTER GÖTTINGEN   (Germany)

Author keywords

cancer related mutations; crystal structure; pre mRNA splicing; SF3b; SF3B1; U2AF65

Indexed keywords

BINDING PROTEIN; SF3B PROTEIN; SF3B10 PROTEIN; SF3B130 PROTEIN; SF3B14B PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG; CDK2AP2 PROTEIN, HUMAN; ONCOPROTEIN; PHOSPHOPROTEIN; PROTEIN BINDING; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; RNA SPLICING FACTOR; SF3B1 PROTEIN, HUMAN; SPLICING FACTOR U2AF; TUMOR PROTEIN; U2AF2 PROTEIN, HUMAN;

ARTICLE; CRYSTAL STRUCTURE; FEMALE; HUMAN; HUMAN CELL; MUTATION; NEOPLASM; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN LOCALIZATION; ALPHA HELIX; AMINO ACID SEQUENCE; ANIMAL; BACULOVIRIDAE; BETA SHEET; BINDING SITE; CHEMISTRY; GENE EXPRESSION; GENETICS; HELA CELL LINE; METABOLISM; MOLECULAR CLONING; MOLECULAR MODEL; MOTH; PROTEIN DOMAIN; PROTEIN SUBUNIT; PROTEIN TERTIARY STRUCTURE; RNA SPLICING; SPLICEOSOME; TUMOR SUPPRESSOR GENE; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; BACULOVIRIDAE; BINDING SITES; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; GENE EXPRESSION; GENES, TUMOR SUPPRESSOR; HELA CELLS; HUMANS; MODELS, MOLECULAR; MOTHS; MUTATION; NEOPLASM PROTEINS; ONCOGENE PROTEINS; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; RNA SPLICING; RNA SPLICING FACTORS; SPLICEOSOMES; SPLICING FACTOR U2AF;

EID: 84992091155     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2016.08.036     Document Type: Article

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