› 2lyv

Solution NMR

Solution structure of the two RRM domains of hnRNP A1 (UP1) using segmental isotope labeling

Released:
DOI: 10.2210/pdb2lyv/pdb
PDB entry 2lyv coloured by chain, ensemble of 20 models, front view.
PDB entry 2lyv coloured by chain, ensemble of 20 models, side view.
PDB entry 2lyv coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology.
Barraud P, Allain FH
J Biomol NMR 55 119-38 (2013)
PMID: 23247503

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 197 amino acids
Theoretical weight: 22.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09651 (Residues: 2-196; Coverage: 52%)
Gene names: HNRNPA1, HNRPA1
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

hnRNP A1: the Swiss army knife of gene expression.
Jean-Philippe et al. (2013)
4 more

13 mentions without citation

The roles of intrinsic disorder-based liquid-liquid phase transitions in the "Dr. Jekyll-Mr. Hyde" behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.
Uversky VN. (2017)
12 more