› 2k72

Solution NMR

Solution NMR structure of toxin-like potassium channel blocking domain in MMP23

Released:
DOI: 10.2210/pdb2k72/pdb
PDB entry 2k72 coloured by chain, ensemble of 20 models, front view.
PDB entry 2k72 coloured by chain, ensemble of 20 models, side view.
PDB entry 2k72 coloured by chain, ensemble of 20 models, top view.
Source organism: Rattus norvegicus
Primary publication:
Potassium channel modulation by a toxin domain in matrix metalloprotease 23.
Rangaraju S, Khoo KK, Feng ZP, Crossley G, Nugent D, Khaytin I, Chi V, Pham C, Calabresi P, Pennington MW, Norton RS, Chandy KG
J Biol Chem 285 9124-36 (2010)
PMID: 19965868

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Matrix metalloproteinase-23, soluble form Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 4.44 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: O88272 (Residues: 254-290; Coverage: 10%)
Gene names: Mifr, Mmp23
Sequence domains: ShK domain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 50%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

12 review citations

Missing the target: matrix metalloproteinase antitargets in inflammation and cancer.
Dufour et al. (2013)
11 more

4 mentions without citation

Structure of the voltage-gated potassium channel KV1.3: Insights into the inactivated conformation and binding to therapeutic leads.
Chandy et al. (2023)
3 more