› 5v87

X-ray diffraction
1.69Å resolution

Crystal structure of LARP1-unique domain DM15 bound to m7GpppC

Released:
DOI: 10.2210/pdb5v87/pdb
PDB entry 5v87 coloured by chain, front view.
PDB entry 5v87 coloured by chain, side view.
PDB entry 5v87 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
La-related protein 1 (LARP1) binds the mRNA cap, blocking eIF4F assembly on TOP mRNAs.
Lahr RM, Fonseca BD, Ciotti GE, Al-Ashtal HA, Jia JJ, Niklaus MR, Blagden SP, Alain T, Berman AJ
Elife 6 (2017)
PMID: 28379136

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
La-related protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 162 amino acids
Theoretical weight: 19.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6PKG0 (Residues: 873-1023; Coverage: 14%)
Gene names: KIAA0731, LARP, LARP1
Sequence domains: LARP1 HEAT repeat region

Ligands and Environments

2 bound ligands:
Ligand MGT 1 x MGT
Ligand 91P 1 x 91P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: P21
Unit cell:
a: 47.959Å b: 59.962Å c: 60.321Å
α: 90° β: 100.65° γ: 90°
R-values:
R R work R free
0.183 0.182 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

28 review citations

Signaling Pathways Involved in the Regulation of mRNA Translation.
Roux et al. (2018)
27 more

4 mentions without citation

LARP1 on TOP of ribosome production.
Fonseca et al. (2018)
3 more