› 1y2o

X-ray diffraction
2.2Å resolution

Structure of N-terminal domain IRSp53/BAIAP2

Released:
DOI: 10.2210/pdb1y2o/pdb
PDB entry 1y2o coloured by chain, front view.
PDB entry 1y2o coloured by chain, side view.
PDB entry 1y2o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53.
Millard TH, Bompard G, Heung MY, Dafforn TR, Scott DJ, Machesky LM, Fütterer K
EMBO J 24 240-50 (2005)
PMID: 15635447

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194065 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BAR/IMD domain-containing adapter protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 28.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UQB8 (Residues: 1-250; Coverage: 45%)
Gene name: BAIAP2
Sequence domains: IRSp53/MIM homology domain
Structure domains: Arfaptin homology (AH) domain/BAR domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P21
Unit cell:
a: 49.879Å b: 64.164Å c: 74.586Å
α: 90° β: 106.18° γ: 90°
R-values:
R R work R free
0.23 0.228 0.267
Expression system: Escherichia coli

Quick links

Citations

40 review citations

Membrane recognition by phospholipid-binding domains.
Lemmon MA. (2008)
39 more

16 mentions without citation

Membrane curvature and its generation by BAR proteins.
Mim et al. (2012)
15 more