Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation
Article Abstract:
The complex formed between the regulatory element of human U1A 3'-untranslated region and the U1A protein RNA-binding domain follows an unanticipated recognition mechanism as revealed by nuclear magnetic resonance structure analysis. The mechanism involves interaction of the variable loops of ribonucleoprotein region with the helical region of RNA. This is followed by folding of the RNA single-stranded loop and reorganization of the C-terminal region, which increases surface complementarity and recognition of the functional group.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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The importance of being unfolded
Article Abstract:
Multidimensional nuclear magnetic resonance was used on transcriptional proteins of Salmonella typhimurium to analyze the biological significance of the unfolded state of proteins. Results have shown that the transcriptional regulator is in an unfolded configuration during its normal physiological state to easily access the protein through the transport channel and thus, perform its regulatory function inside the cytoplasm.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Crystal structure of the spliceosomal U2B"-U2A' protein complex bound to a fragment of U2 small nuclear RNA
Article Abstract:
Research has established the crystal structure of a ternary protein complex situated next to the spliceosomal U2B"-U2A' protein complex and hairpin-loop IV of U2 small nuclear RNA. The amino-acid sequences of the RNA binding site and U2B" and U2A' proteins are illustrated. The crystal structure was observed at 2.4 angstroms resolution. X-ray structure measurements are listed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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