› 2a05

Solution NMR

The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates Ryanodine receptor Ca2+ signaling

Released:
DOI: 10.2210/pdb2a05/pdb
PDB entry 2a05 coloured by chain, ensemble of 23 models, front view.
PDB entry 2a05 coloured by chain, ensemble of 23 models, side view.
PDB entry 2a05 coloured by chain, ensemble of 23 models, top view.
Source organism: Mus musculus
Primary publication:
The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signaling.
Gibbs GM, Scanlon MJ, Swarbrick J, Curtis S, Gallant E, Dulhunty AF, O'Bryan MK
J Biol Chem 281 4156-63 (2006)
PMID: 16339766

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine-rich secretory protein 2 Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.12 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P16563 (Residues: 189-243; Coverage: 25%)
Gene names: Crisp2, Tpx-1, Tpx1
Sequence domains: Crisp
Structure domains: Crisp domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Automated Resonance assignment using Torsion Angle Dynamics (CANDID), Further refinement with CA and CB chem shifts and database potentials
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Emerging Insights into the Functions of Pathogenesis-Related Protein 1.
Breen et al. (2017)
13 more

3 mentions without citation

Potassium channel modulation by a toxin domain in matrix metalloprotease 23.
Rangaraju et al. (2010)
2 more