› 1qag

X-ray diffraction
3Å resolution

Actin binding region of the dystrophin homologue utrophin

Released:
DOI: 10.2210/pdb1qag/pdb
PDB entry 1qag coloured by chain, front view.
PDB entry 1qag coloured by chain, side view.
PDB entry 1qag coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer.
Keep NH, Winder SJ, Moores CA, Walke S, Norwood FL, Kendrick-Jones J
Structure 7 1539-46 (1999)
PMID: 10647184

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-155560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Utrophin Chains: A, B
Molecule details ›
Chains: A, B
Length: 226 amino acids
Theoretical weight: 26.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P46939 (Residues: 31-256; Coverage: 7%)
Gene names: DMDL, DRP1, UTRN
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 150.145Å b: 55.16Å c: 80.42Å
α: 90° β: 106.06° γ: 90°
R-values:
R R work R free
0.198 0.198 0.258
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Function and genetics of dystrophin and dystrophin-related proteins in muscle.
Blake et al. (2002)
8 more

13 mentions without citation

An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function.
Volkmann et al. (2001)
12 more