› 4a4f

Solution NMR

Solution structure of SPF30 Tudor domain in complex with symmetrically dimethylated arginine

Released:
DOI: 10.2210/pdb4a4f/pdb
PDB 4a4f coloured by chain and viewed from the front.
PDB 4a4f coloured by chain and viewed from the side.
PDB 4a4f coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins.
Tripsianes K, Madl T, Machyna M, Fessas D, Englbrecht C, Fischer U, Neugebauer KM, Sattler M
Nat Struct Mol Biol 18 1414-20 (2011)
PMID: 22101937

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Survival of motor neuron-related-splicing factor 30 Chain: A
Molecule details ›
Chain: A
Length: 64 amino acids
Theoretical weight: 6.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75940 (Residues: 65-128; Coverage: 27%)
Gene names: SMNDC1, SMNR, SPF30
Sequence domains: Survival motor neuron protein (SMN)
Structure domains: SH3 type barrels.

Ligands and Environments

1 bound ligand:
Ligand 2MR 1 x 2MR
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 86%
Refinement method: simulated annealing
Chemical shifts: BMR18006  
Expression system: Escherichia coli

Quick links

Citations

29 review citations

A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly.
Chen et al. (2022)
28 more

1 mention without citation

Crystal structure of TDRD3 and methyl-arginine binding characterization of TDRD3, SMN and SPF30.
Liu et al. (2012)