ISSN:
1573-5001
Keywords:
RNP domain
;
RNA–protein interactions
;
U1A protein
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
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 Å (for all ordered regions), and 1.08 Å 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. Abbreviations: hnRNP, heterologous nuclear ribonucleoprotein; mRNA, messenger RNA; RNP, ribonucleoprotein; U1A-102, amino acids 2–102 of human U1A protein containing the mutations Tyr31His and Gln36Arg; U1A-117, amino acids 2–117 of human U1A protein; PIE–RNA, polyadenylation inhibition element RNA. To aid the distinction between protein and RNA in the text, amino acid residues are referred to using their three-letter codes throughout, except in the figures and Tables 1 and 4a (where the single-letter code is used to save space).
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008297502874
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