› 2d1l

X-ray diffraction
1.85Å resolution

Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)

Released:
DOI: 10.2210/pdb2d1l/pdb
PDB entry 2d1l coloured by chain, front view.
PDB entry 2d1l coloured by chain, side view.
PDB entry 2d1l coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural basis for the actin-binding function of missing-in-metastasis.
Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R
Structure 15 145-55 (2007)
PMID: 17292833

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185877 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein MTSS 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 253 amino acids
Theoretical weight: 28.99 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8R1S4 (Residues: 1-250; Coverage: 33%)
Gene names: Mim, Mtss1
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 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P21
Unit cell:
a: 53.503Å b: 37.319Å c: 129.016Å
α: 90° β: 94.07° γ: 90°
R-values:
R R work R free
0.186 0.183 0.228
Expression system: Escherichia coli BL21

Quick links

Citations

25 review citations

Filopodia: molecular architecture and cellular functions.
Mattila et al. (2008)
24 more

10 mentions without citation

Missing-in-metastasis and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain-like mechanism.
Mattila et al. (2007)
9 more