› 1m1x

X-ray diffraction
3.3Å resolution

CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+

Released:
DOI: 10.2210/pdb1m1x/pdb
PDB entry 1m1x coloured by chain, front view.
PDB entry 1m1x coloured by chain, side view.
PDB entry 1m1x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand.
Xiong JP, Stehle T, Zhang R, Joachimiak A, Frech M, Goodman SL, Arnaout MA
Science 296 151-5 (2002)
PMID: 11884718

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138434 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Integrin alpha-V Chain: A
Molecule details ›
Chain: A
Length: 957 amino acids
Theoretical weight: 105.88 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P06756 (Residues: 31-987; Coverage: 94%)
Gene names: ITGAV, MSK8, VNRA, VTNR
Sequence domains:
Structure domains:
Integrin beta-3 Chain: B
Molecule details ›
Chain: B
Length: 692 amino acids
Theoretical weight: 76.65 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P05106 (Residues: 27-718; Coverage: 91%)
Gene names: GP3A, ITGB3
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, NDG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 4 x NAG
Ligand MN 6 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 130.4Å b: 130.4Å c: 310.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.244 0.323
Expression system: Spodoptera frugiperda

Quick links

Citations

198 review citations

Integrins: bidirectional, allosteric signaling machines.
Hynes RO. (2002)
197 more

6 mentions without citation

Extracellular membrane-proximal domain of HAb18G/CD147 binds to metal ion-dependent adhesion site (MIDAS) motif of integrin β1 to modulate malignant properties of hepatoma cells.
Li et al. (2012)
5 more