› 2opu

Solution NMR

Solution NMR Structure of the First Domain of KSRP

Released:
DOI: 10.2210/pdb2opu/pdb
PDB entry 2opu coloured by chain, ensemble of 25 models, front view.
PDB entry 2opu coloured by chain, ensemble of 25 models, side view.
PDB entry 2opu coloured by chain, ensemble of 25 models, top view.
Source organism: Homo sapiens
Primary publication:
Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding.
Díaz-Moreno I, Hollingworth D, Frenkiel TA, Kelly G, Martin S, Howell S, García-Mayoral M, Gherzi R, Briata P, Ramos A
Nat Struct Mol Biol 16 238-46 (2009)
PMID: 19198587

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-187817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Far upstream element-binding protein 2 Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 9.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92945 (Residues: 130-218; Coverage: 13%)
Gene names: FUBP2, KHSRP
Sequence domains: KH domain
Structure domains: K Homology domain, type 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

The role of the 3' untranslated region in post-transcriptional regulation of protein expression in mammalian cells.
Matoulkova et al. (2012)
17 more

5 mentions without citation

Diverse roles of the nucleic acid-binding protein KHSRP in cell differentiation and disease.
Briata et al. (2016)
4 more