› 2m68

Solution NMR

NMR solution structure ensemble of 3-4D mutant domain 11 IGF2R in complex with IGF2 (domain 11 structure only)

Released:
DOI: 10.2210/pdb2m68/pdb
PDB entry 2m68 coloured by chain, ensemble of 20 models, front view.
PDB entry 2m68 coloured by chain, ensemble of 20 models, side view.
PDB entry 2m68 coloured by chain, ensemble of 20 models, 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: 15.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Escherichia coli

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)