The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. [electronic resource]
- Nature structural biology Apr 2000
- 329-35 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1072-8368
10.1038/74101 doi
3' Untranslated Regions--chemistry Allosteric Regulation Amino Acid Sequence Base Sequence Binding Sites Humans Models, Molecular Molecular Sequence Data Molecular Weight Nuclear Magnetic Resonance, Biomolecular Nucleic Acid Conformation Poly A--metabolism Polynucleotide Adenylyltransferase--antagonists & inhibitors Protein Binding Protein Structure, Secondary RNA Processing, Post-Transcriptional--genetics RNA, Messenger--chemistry RNA-Binding Proteins--chemistry Regulatory Sequences, Nucleic Acid--genetics Ribonucleoprotein, U1 Small Nuclear--chemistry Structure-Activity Relationship Substrate Specificity