› 3nw6

X-ray diffraction
2.2Å resolution

Crystal structure of insulin-like growth factor 1 receptor (IGF-1R-WT) complex with a carbon-linked proline isostere inhibitor (11A)

Released:
DOI: 10.2210/pdb3nw6/pdb
PDB entry 3nw6 coloured by chain, front view.
PDB entry 3nw6 coloured by chain, side view.
PDB entry 3nw6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Proline isosteres in a series of 2,4-disubstituted pyrrolo[1,2-f][1,2,4]triazine inhibitors of IGF-1R kinase and IR kinase.
Sampognaro AJ, Wittman MD, Carboni JM, Chang C, Greer AF, Hurlburt WW, Sack JS, Vyas DM
Bioorg Med Chem Lett 20 5027-30 (2010)
PMID: 20675137

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139909 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Insulin-like growth factor 1 receptor beta chain Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 35.04 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: P08069 (Residues: 982-1286; Coverage: 23%)
Gene name: IGF1R
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand LGW 1 x LGW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: C2
Unit cell:
a: 107.308Å b: 41.161Å c: 79.173Å
α: 90° β: 121.05° γ: 90°
R-values:
R R work R free
0.184 0.18 0.252
Expression system: unidentified baculovirus

Quick links

Citations

9 citation in other articles

Serine phosphorylation of the insulin-like growth factor I (IGF-1) receptor C-terminal tail restrains kinase activity and cell growth.
Kelly et al. (2012)
8 more

7 mentions without citation

Gourds and squashes (Cucurbita spp.) adapted to megafaunal extinction and ecological anachronism through domestication.
Kistler et al. (2015)
6 more