|Entry||Database: PDB / ID: 1dz5|
|Title||The NMR structure of the 38KDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein|
|Keywords||RIBONUCLEOPROTEIN/RNA / RIBONUCLEOPROTEIN-RNA COMPLEX / POLYADENYLATION / PROTEIN PROTEIN INTERACTION / RNA PROTEIN INTERACTION|
|Function / homology|
Function and homology information
mRNA Splicing - Major Pathway / regulation of mRNA polyadenylation / U1 snRNP binding / U1 snRNP / U1 snRNA binding / spliceosomal complex / mRNA splicing, via spliceosome / RNA binding / nucleoplasm / identical protein binding
RNA recognition motif domain / RNA-binding domain superfamily / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain) / Nucleotide-binding alpha-beta plait domain superfamily / U1 small nuclear ribonucleoprotein A, RNA recognition motif 1 / U1 small nuclear ribonucleoprotein A, RNA recognition motif 2
U1 small nuclear ribonucleoprotein A
|Biological species||HOMO SAPIENS (human)|
|Method||SOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS|
|Authors||Varani, L. / Gunderson, S.I. / Mattaj, I.W. / Kay, L.E. / Neuhaus, D. / Varani, G.|
|Citation||Journal: Nat.Struct.Biol. / Year: 2000|
Title: The NMR Structure of the 38kDa U1A Protein-Pie RNA Complex Reveals the Basis of Cooperativity in Regulation of Polyadenylation by Human U1A Protein
Authors: Varani, L. / Gunderson, S.I. / Mattaj, I.W. / Kay, L.E. / Neuhaus, D. / Varani, G.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A
B: U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A
C: PIE, RNA (5'-R(*GP*AP*GP*AP*CP*AP*UP*UP*GP*CP*AP*CP*CP* CP*GP*GP*AP*GP*UP*CP*UP*C)-3')
D: PIE, RNA (5'-R(*GP*AP*GP*AP*CP*AP*UP*UP*GP*CP*AP*CP*CP* CP*GP*GP*AP*GP*UP*CP*UP*C)-3')
Mass: 11613.582 Da / Num. of mol.: 2 / Fragment: RESIDUES 2-102 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET13A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P09012
|#2: RNA chain|
Mass: 7033.242 Da / Num. of mol.: 2 / Fragment: 3' UTR POLYADENYLATION INHIBITION ELEMENT / Mutation: YES / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / Details: PRODUCED BY IN VITRO TRANSCRIPTION
|Compound details||MUTATIONS IN CHAIN A,B: Y31H, Q36R MUTATIONS IN CHAIN C: U18C, A21G MUTATIONS IN CHAIN D: U47C|
|Experiment||Method: SOLUTION NMR|
Conditions-ID: 1 / Solution-ID: 1
|NMR details||Text: THE STRUCTURE WAS DETERMINED USING 15N, 13C AND 2D LABELED SAMPLES. DIFFERENT LABELLED SPECIES WERE MIXED IN DIFFERENT EXPERIMENTS. TRIPLE RESONANCE EXPERIMENTS COULD NOT BE USED DUE TO THE SIZE OF THE COMPLEX; TROSY WAS NOT AVAILABLE WHEN MOST OF THE ASSIGNMENT WAS COMPLETED.|
|Details||Contents: 10MM PHOSPHATE BUFFER|
|Sample conditions||Ionic strength: 10MM PHOSPHATE BUFFER / pH: 6.0 / Pressure: 1 atm / Temperature: 300 K|
*PLUSMethod: other / Details: NMR
|NMR spectrometer||Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz|
|Refinement||Method: RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1 / Details: DETAILS CAN BE FOUND IN THE JOURNAL CITATION ABOVE|
|NMR ensemble||Conformer selection criteria: AGREEMENT WITH EXPERIMENTAL DATA|
Conformers calculated total number: 50 / Conformers submitted total number: 13
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