› 1lmr

Solution NMR

Solution of ADO1, a Toxin from the Assassin Bugs Agriosphodrus dohrni that Blocks the Voltage Sensitive Calcium Channel L-type

Released:
DOI: 10.2210/pdb1lmr/pdb
PDB entry 1lmr coloured by chain, ensemble of 21 models, front view.
PDB entry 1lmr coloured by chain, ensemble of 21 models, side view.
PDB entry 1lmr coloured by chain, ensemble of 21 models, top view.
Source organism: Agriosphodrus dohrni
Primary publication:
Solution structure of ADO1, a toxin extracted from the saliva of the assassin bug, Agriosphodrus dohrni.
Bernard C, Corzo G, Adachi-Akahane S, Foures G, Kanemaru K, Furukawa Y, Nakajima T, Darbon H
Proteins 54 195-205 (2004)
PMID: 14696181

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Toxin Ado1 Chain: A
Molecule details ›
Chain: A
Length: 35 amino acids
Theoretical weight: 3.79 KDa
Source organism: Agriosphodrus dohrni
UniProt:
  • Canonical: P58608 (Residues: 1-35; Coverage: 100%)
Sequence domains: Ptu family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing

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Citations

1 review citation

Toxin structures as evolutionary tools: Using conserved 3D folds to study the evolution of rapidly evolving peptides.
Undheim et al. (2016)
6 other articles

1 mention without citation

Identification of distant Agouti-like sequences and re-evaluation of the evolutionary history of the Agouti-related peptide (AgRP).
Västermark et al. (2012)