RNA-protein interactions.
Recent discoveries have revealed that there is a myriad of RNAs and associated RNA-binding proteins that spatially and temporally appear in the cells of all organisms. The structures of these RNA-protein complexes are providing valuable insights into the binding modes and functional implications of these interactions. Even the common RNA-binding domains (RBDs) and the double stranded RNA binding motifs (dsRBMs) have been shown to exhibit a plethora of binding modes.
Department of Biochemistry and Molecular Biophysics, Box 8231, Washington University School of Medicine, 660 South Euclid Avenue, St Louis, MO 63110, USA. hall@bionmer3.wustl.edu
Kathleen B
KB
Hall
D000243:Adenosine Deaminase / Q000378:metabolism; D051959:ELAV Proteins; D015801:Helminth Proteins / Q000378:metabolism; D006801:Humans; D009124:Muscle Proteins / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism; D039502:Nuclear Cap-Binding Protein Complex / Q000378:metabolism; D009687:Nuclear Proteins; D010750:Phosphoproteins / Q000378:metabolism; D038941:Polypyrimidine Tract-Binding Protein / Q000378:metabolism; D011485:Protein Binding; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism; D000072668:Splicing Factor U2AF; D019892:eIF-2 Kinase / Q000378:metabolism; D000097796:Nucleolin; D000096985:Calponins
D000243:Adenosine Deaminase; D051959:ELAV Proteins; D015801:Helminth Proteins; D009124:Muscle Proteins; D009419:Nerve Tissue Proteins; D039502:Nuclear Cap-Binding Protein Complex; D009687:Nuclear Proteins; D010750:Phosphoproteins; D038941:Polypyrimidine Tract-Binding Protein; D012313:RNA; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D000072668:Splicing Factor U2AF; D019892:eIF-2 Kinase; D000097796:Nucleolin; C076753:U2AF1 protein, human; C118619:calponin homolog protein, Schistosoma japonicum; D000096985:Calponins