› 1mb8

X-ray diffraction
2.15Å resolution

Crystal Structure of the actin binding domain of plectin

Released:
DOI: 10.2210/pdb1mb8/pdb
PDB entry 1mb8 coloured by chain, front view.
PDB entry 1mb8 coloured by chain, side view.
PDB entry 1mb8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4.
García-Alvarez B, Bobkov A, Sonnenberg A, de Pereda JM
Structure 11 615-25 (2003)
PMID: 12791251

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172226 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plectin Chain: A
Molecule details ›
Chain: A
Length: 243 amino acids
Theoretical weight: 28.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15149 (Residues: 174-195, 196-403; Coverage: 5%)
Gene names: PLEC, PLEC1
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 33.597Å b: 79.283Å c: 82.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.261
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Current insights into the formation and breakdown of hemidesmosomes.
Litjens et al. (2006)
14 more

13 mentions without citation

Opening of tandem calponin homology domains regulates their affinity for F-actin.
Galkin et al. (2010)
12 more