› 5mf9

Solution NMR

Solution structure of the RBM5 OCRE domain in complex with polyproline SmN peptide.

Released:
DOI: 10.2210/pdb5mf9/pdb
PDB entry 5mf9 coloured by chain, ensemble of 10 models, front view.
PDB entry 5mf9 coloured by chain, ensemble of 10 models, side view.
PDB entry 5mf9 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the recognition of spliceosomal SmN/B/B' proteins by the RBM5 OCRE domain in splicing regulation.
Mourão A, Bonnal S, Soni K, Warner L, Bordonné R, Valcárcel J, Sattler M
Elife 5 (2016)
PMID: 27894420

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156628 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA-binding protein 5 Chain: A
Molecule details ›
Chain: A
Length: 64 amino acids
Theoretical weight: 7.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P52756 (Residues: 451-511; Coverage: 8%)
Gene names: H37, LUCA15, RBM5
Sequence domains: OCRE domain
Survival motor neuron protein Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Integrated structural biology to unravel molecular mechanisms of protein-RNA recognition.
Schlundt et al. (2017)
2 more

2 mentions without citation

Do polyproline II helix associations modulate biomolecular condensates?
Mompeán et al. (2021)
1 more