› 2r0z

X-ray diffraction
2.1Å resolution

PFA1 FAB complexed with GripI peptide fragment

Released:
DOI: 10.2210/pdb2r0z/pdb
PDB entry 2r0z coloured by chain, front view.
PDB entry 2r0z coloured by chain, side view.
PDB entry 2r0z coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Molecular basis for passive immunotherapy of Alzheimer's disease.
Gardberg AS, Dice LT, Ou S, Rich RL, Helmbrecht E, Ko J, Wetzel R, Myszka DG, Patterson PH, Dealwis C
Proc Natl Acad Sci U S A 104 15659-64 (2007)
PMID: 17895381

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-207559 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ig-like domain-containing protein Chain: L
Molecule details ›
Chain: L
Length: 219 amino acids
Theoretical weight: 24.2 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: A2NHM3 (Residues: 1-219; Coverage: 100%)
Gene names: Igk-C, Igkc
Sequence domains:
Structure domains: Immunoglobulins
IgG2a Fab fragment heavy chain, Fd portion Chain: H
Molecule details ›
Chain: H
Length: 223 amino acids
Theoretical weight: 24 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
GripI peptide fragment Chain: Q
Molecule details ›
Chain: Q
Length: 6 amino acids
Theoretical weight: 776 Da

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
1 modified residue:
Ligand YCM 1 x YCM

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU, APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 41.467Å b: 112.243Å c: 43.174Å
α: 90° β: 93.43° γ: 90°
R-values:
R R work R free
0.204 0.201 0.261

Quick links

Citations

18 review citations

The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes.
Benilova et al. (2012)
17 more

1 mention without citation

Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes.
Ma et al. (2016)