› 2mzq

Solution NMR

NMR structure of the RRM3 domain of Gbp2

Released:
DOI: 10.2210/pdb2mzq/pdb
PDB entry 2mzq coloured by chain, ensemble of 20 models, front view.
PDB entry 2mzq coloured by chain, ensemble of 20 models, side view.
PDB entry 2mzq coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Gbp2 interacts with THO/TREX through a novel type of RRM domain.
Martínez-Lumbreras S, Taverniti V, Zorrilla S, Séraphin B, Pérez-Cañadillas JM
OpenAccess logo Nucleic Acids Res 44 437-48 (2016)
PMID: 26602689

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-150504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/arginine (SR)-type shuttling mRNA binding protein GBP2 Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 11.09 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P25555 (Residues: 329-427; Coverage: 23%)
Gene names: GBP2, RLF6, YCL011C, YCL11C
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: 88%
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The role of TREX in gene expression and disease.
Heath et al. (2016)
14 other articles

1 mention without citation

Gbp2 interacts with THO/TREX through a novel type of RRM domain.
Martínez-Lumbreras et al. (2016)