› 2kq6

Solution NMR

The structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity

Released:
DOI: 10.2210/pdb2kq6/pdb
PDB entry 2kq6 coloured by chain, ensemble of 20 models, front view.
PDB entry 2kq6 coloured by chain, ensemble of 20 models, side view.
PDB entry 2kq6 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity.
Petri ET, Celic A, Kennedy SD, Ehrlich BE, Boggon TJ, Hodsdon ME
Proc Natl Acad Sci U S A 107 9176-81 (2010)
PMID: 20439752

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171759 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polycystin-2 Chain: A
Molecule details ›
Chain: A
Length: 78 amino acids
Theoretical weight: 9.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13563 (Residues: 720-797; Coverage: 8%)
Gene names: PKD2, TRPP2
Structure domains: EF-hand

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 68%
Refinement method: XPLOR-NIH
Expression system: Escherichia coli

Quick links

Citations

17 review citations

A polycystin-centric view of cyst formation and disease: the polycystins revisited.
Ong et al. (2015)
16 more

6 mentions without citation

Structural biology of TRP channels.
Hellmich et al. (2014)
5 more