The N-terminal domain of Nup159 forms a β-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore

Molecular Cell

Volumn 16, Issue 5, 2004, Pages 749-760

  Weirich, Christine S ^a   Erzberger, Jan P ^a   Berger, James M ^a   Weis, Karsten ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HELICASE; HELICASE DBP5; MESSENGER RNA; NUCLEOPORIN; NUCLEOPORIN 159; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CELL NUCLEUS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOPLASM; ENZYME LOCALIZATION; EUKARYOTE; GENE MUTATION; GENE TARGETING; GENETIC ANALYSIS; GENETIC CONSERVATION; MOLECULE; MUTAGENESIS; NONHUMAN; NUCLEAR PORE; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; SURFACE PROPERTY;

ADENOSINE TRIPHOSPHATASES; BIOLOGICAL TRANSPORT; CELL NUCLEUS; CHROMATOGRAPHY, GEL; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; DEAD-BOX RNA HELICASES; IN SITU HYBRIDIZATION; MUTAGENESIS, SITE-DIRECTED; MUTATION; NUCLEAR PORE; NUCLEAR PORE COMPLEX PROTEINS; NUCLEOCYTOPLASMIC TRANSPORT PROTEINS; PLASMIDS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; RNA HELICASES; RNA, MESSENGER; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EUKARYOTA;

EID: 9744266768     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.10.032     Document Type: Article

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