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.
Varani, L
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
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