› 1mcw

X-ray diffraction
3.5Å resolution

THREE-DIMENSIONAL STRUCTURE OF A HYBRID LIGHT CHAIN DIMER. PROTEIN ENGINEERING OF A BINDING CAVITY

Released:
DOI: 10.2210/pdb1mcw/pdb
PDB 1mcw coloured by chain and viewed from the front.
PDB 1mcw coloured by chain and viewed from the side.
PDB 1mcw coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Three-dimensional structure of a hybrid light chain dimer: protein engineering of a binding cavity.
Ely KR, Herron JN, Edmundson AB
Mol. Immunol. 27 101-14 (1990)
PMID: 2108322

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
IMMUNOGLOBULIN WEIR (LIGHT CHAIN) Chain: W
Molecule details ›
Chain: W
Length: 216 amino acids
Theoretical weight: 22.91 KDa
Source organism: Homo sapiens
Structure domains: Immunoglobulins
Immunoglobulin lambda variable 2-8 Chain: M
Molecule details ›
Chain: M
Length: 216 amino acids
Theoretical weight: 22.83 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01709 (Residues: 20-118; Coverage: 100%)
Gene name: IGLV2-8
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 72.3Å b: 72.3Å c: 185.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 not available not available

Quick links

Citations

3 review citations

Immunoglobulin light chain amyloid aggregation.
Blancas-Mejia et al. (2018)
2 more

1 mention without citation

Exceptional amyloid beta peptide hydrolyzing activity of nonphysiological immunoglobulin variable domain scaffolds.
Taguchi et al. (2008)