› 3neq

X-ray diffraction
1.25Å resolution

Crystal structure of the chimeric muscarinic toxin MT7 with loop 3 from MT1

Released:
DOI: 10.2210/pdb3neq/pdb
PDB entry 3neq coloured by chain, front view.
PDB entry 3neq coloured by chain, side view.
PDB entry 3neq coloured by chain, top view.
Source organism: Dendroaspis angusticeps
Primary publication:
Engineering of three-finger fold toxins creates ligands with original pharmacological profiles for muscarinic and adrenergic receptors.
Fruchart-Gaillard C, Mourier G, Blanchet G, Vera L, Gilles N, Ménez R, Marcon E, Stura EA, Servent D
PLoS One 7 e39166 (2012)
PMID: 22720062

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-160470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Muscarinic toxin 1; Muscarinic toxin 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 66 amino acids
Theoretical weight: 7.6 KDa
Source organism: Dendroaspis angusticeps
Expression system: Not provided
UniProt:
  • Canonical: Q8QGR0 (Residues: 22-69, 80-86; Coverage: 85%)
  • Canonical: P81030 (Residues: 49-59; Coverage: 17%)
Structure domains: CD59

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 25.82Å b: 56.578Å c: 80.709Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.147 0.168
Expression system: Not provided

Quick links

Citations

3 review citations

The three-finger toxin fold: a multifunctional structural scaffold able to modulate cholinergic functions.
Kessler et al. (2017)
2 more

5 mentions without citation

The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain.
Mysling et al. (2016)
4 more