ArticleJournal of biomolecular NMR1998
Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element.
Article in Journal of biomolecular NMR, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Biochemical and NMR analyses of an SF3b155-p14-U2AF-RNA interaction network involved in branch point definition during pre-mRNA splicing.RNA (New York, N.Y.) · 2006Article
- A binding mechanism in protein-nucleotide interactions: implication for U1A RNA binding.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III.The EMBO journal · 2004Article
- Determinants within an 18-amino-acid U1A autoregulatory domain that uncouple cooperative RNA binding, inhibition of polyadenylation, and homodimerization.Molecular and cellular biology · 2003Article
- Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin.The EMBO journal · 2000Article
- Interactions of a didomain fragment of the Drosophila sex-lethal protein with single-stranded uridine-rich oligoribonucleotides derived from the transformer and Sex-lethal messenger RNA precursors: NMR with residue-selective [5-2H]uridine substitutions.Journal of biomolecular NMR · 2000Article
- RNA recognition by a Staufen double-stranded RNA-binding domain.The EMBO journal · 2000Article
- Refinement of the structure of protein-RNA complexes by residual dipolar coupling analysis.Journal of biomolecular NMR · 1999Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA-protein recognition is critical to post-transcriptional regulation of gene expression, yet poorly understood at the molecular level. The relatively slow progress in understanding this important area of molecular biology is due to difficulties in obtaining good-quality crystals and derivatives, and in preparing samples suitable for NMR investigation. The determination of the structure of the complex between the human U1A protein and its polyadenylation inhibition element is described here. In this paper, we describe the sample preparation, spectral assignments, construction of the NOE-based distance constraints and methodology for calculating the structure of the complex. The structure was determined to an overall precision of 2.03 A (for all ordered regions), and 1.08 A for the protein-RNA interface. The patterns of hydrogen bonding and hydrophobic interactions at the interface were analysed statistically using the final ensemble of 31 structures.
Indexed as
Identifiers
9566313What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.