› 2oex

X-ray diffraction
2.58Å resolution

Structure of ALIX/AIP1 V Domain

Released:
DOI: 10.2210/pdb2oex/pdb
PDB entry 2oex coloured by chain, front view.
PDB entry 2oex coloured by chain, side view.
PDB entry 2oex coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding.
Fisher RD, Chung HY, Zhai Q, Robinson H, Sundquist WI, Hill CP
Cell 128 841-52 (2007)
PMID: 17350572

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Programmed cell death 6-interacting protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 39.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WUM4 (Residues: 360-702; Coverage: 40%)
Gene names: AIP1, ALIX, KIAA1375, PDCD6IP
Sequence domains: ALIX V-shaped domain binding to HIV
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 63.861Å b: 50.049Å c: 130.171Å
α: 90° β: 101.13° γ: 90°
R-values:
R R work R free
0.231 0.228 0.302
Expression system: Escherichia coli

Quick links

Citations

64 review citations

Specificities of secretion and uptake of exosomes and other extracellular vesicles for cell-to-cell communication.
Mathieu et al. (2019)
63 more

3 mentions without citation

The yeast Alix homolog Bro1 functions as a ubiquitin receptor for protein sorting into multivesicular endosomes.
Pashkova et al. (2013)
2 more