Structure of a yeast Dyn2-Nup159 complex and molecular basis for dynein light chain-nuclear pore interaction

Journal of Biological Chemistry

Volumn 287, Issue 19, 2012, Pages 15862-15873

  Romes, Erin M ^a,b   Tripathy, Ashutosh ^a   Slep, Kevin C ^b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASYMMETRIC TRAFFIC; BINDING MODES; BIOCHEMICAL INTERACTIONS; CALORIMETRIC ANALYSIS; COMPLEX FORMATIONS; COMPOSITE SUBSTRATE; FIBRIL ARCHITECTURE; HOMODIMERIZATION; HOMODIMERS; INTERDIMER INTERACTIONS; ISOTHERMAL TITRATION; LIGHT CHAIN; MOLECULAR BASIS; MULTIVALENT BINDING; NUCLEAR PORE COMPLEXES; NUCLEOCYTOPLASMIC TRANSPORT; STRAND STRUCTURE; STRUCTURAL INFORMATION; SYMMETRIC CHANNELS; TARGET SITES;

BINDING ENERGY; BINDING SITES; OLIGOMERIZATION; OLIGOMERS; PEPTIDES;

YEAST;

DYN2 PROTEIN; DYNEIN ADENOSINE TRIPHOSPHATASE; DYNEIN ADENOSINE TRIPHOSPHATASE LIGHT CHAIN; FUNGAL PROTEIN; NUCLEOPORIN; NUP159 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; DNA FLANKING REGION; HOMODIMERIZATION; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PLASTICITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE;

ACYLTRANSFERASES; AMINO ACID SEQUENCE; BINDING SITES; BINDING, COMPETITIVE; CALORIMETRY; CRYSTALLOGRAPHY, X-RAY; DYNEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; NUCLEAR PORE; NUCLEAR PORE COMPLEX PROTEINS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

METAZOA; SACCHAROMYCES CEREVISIAE;

EID: 84860848799     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.336172     Document Type: Article

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