› 5iei

X-ray diffraction
2.8Å resolution

X-ray crystallographic structure of a high affinity IGF2 antagonist (Domain11 AB5 RHH) based on human IGF2R domain 11

Released:
DOI: 10.2210/pdb5iei/pdb
PDB entry 5iei coloured by chain, front view.
PDB entry 5iei coloured by chain, side view.
PDB entry 5iei coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functional evolution of IGF2:IGF2R domain 11 binding generates novel structural interactions and a specific IGF2 antagonist.
Frago S, Nicholls RD, Strickland M, Hughes J, Williams C, Garner L, Surakhy M, Maclean R, Rezgui D, Prince SN, Zaccheo OJ, Ebner D, Sanegre S, Yu S, Buffa FM, Crump MP, Hassan AB
Proc Natl Acad Sci U S A 113 E2766-75 (2016)
PMID: 27140600

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145907 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cation-independent mannose-6-phosphate receptor Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 15.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11717 (Residues: 1508-1649; Coverage: 6%)
Gene names: IGF2R, MPRI
Sequence domains: Cation-independent mannose-6-phosphate receptor repeat
Structure domains: Mannose-6-phosphate receptor binding domain

Ligands and Environments

3 bound ligands:
Ligand GOL 1 x GOL
Ligand EDO 2 x EDO
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 42.12Å b: 48.56Å c: 62.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.222 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Insulin Receptor Isoforms in Physiology and Disease: An Updated View.
Belfiore et al. (2017)
4 more

1 mention without citation

Functional evolution of IGF2:IGF2R domain 11 binding generates novel structural interactions and a specific IGF2 antagonist.
Frago et al. (2016)