Four KH domains of the C. elegans Bicaudal-C ortholog GLD-3 form a globular structural platform

RNA

Volumn 16, Issue 11, 2010, Pages 2058-2067

  Nakel, Katharina ^a   Hartung, Sophia A ^b   Bonneau, Fabien ^a   Eckmann, Christian R ^c   Conti, Elena ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^c MAX PLANCK INSTITUTE OF MOLECULAR CELL BIOLOGY AND GENETICS   (Germany)

Author keywords

Germline development; Post translational control; Protein protein interaction; RNA binding protein; SAXS

Indexed keywords

CYTOPLASM PROTEIN; DIMER; GLOBULAR PROTEIN; MESSENGER RNA; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; PROTEIN GLD 2; PROTEIN GLD 3; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CAENORHABDITIS ELEGANS; CROSS LINKING; CRYSTAL STRUCTURE; EMBRYO DEVELOPMENT; GENE TARGETING; MOLECULAR RECOGNITION; NONHUMAN; POLYADENYLATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN RNA BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RNA-BINDING PROTEINS; SEQUENCE ALIGNMENT;

CAENORHABDITIS ELEGANS;

EID: 78149325316     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.2315010     Document Type: Article

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