PDBsum entry 2kle

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protein links
Membrane protein PDB id
Protein chain
73 a.a. *
* Residue conservation analysis
PDB id:
Name: Membrane protein
Title: Isic refined solution structure of the calcium binding domain of thE C-terminal cytosolic domain of polycystin-2
Structure: Polycystin-2. Chain: a. Fragment: residues 680-796. Synonym: polycystic kidney disease 2 protein, autosomal dominant polycystic kidney disease type ii protein, polycystwin, r48321. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pkd2. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 10 models
Authors: H.R.Kalbitzer
Key ref: F.H.Schumann et al. (2009). NMR-assignments of a cytosolic domain of the C-terminus of polycystin-2. Biomol NMR Assign, 3, 141-144. PubMed id: 19636966 DOI: 10.1007/s12104-009-9160-x
01-Jul-09     Release date:   28-Jul-09    
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Protein chain
Pfam   ArchSchema ?
Q13563  (PKD2_HUMAN) -  Polycystin-2
968 a.a.
73 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium ion binding     1 term  


DOI no: 10.1007/s12104-009-9160-x Biomol NMR Assign 3:141-144 (2009)
PubMed id: 19636966  
NMR-assignments of a cytosolic domain of the C-terminus of polycystin-2.
F.H.Schumann, H.Hoffmeister, M.Schmidt, R.Bader, E.Besl, R.Witzgall, H.R.Kalbitzer.
Mutations in the PKD2 gene lead to the development of polycystic kidney disease (PKD). The PKD2 gene codes for polycystin-2, a cation channel with unknown function. The cytoplasmic, C-terminal domain interacts with a large number of proteins including mDia1, alpha-actinin, PIGEA-14, troponin, and tropomyosin. The C-terminal fragment polycystin-2 (680-796) consisting of 117 amino acids contains a putative calcium binding EF-hand. It was produced in Escherichia coli and enriched uniformly with (13)C and (15)N. The backbone and side chain resonances were assigned by multidimensional NMR methods, the obtained chemical shifts are typical for a partially folded protein. The chemical shifts obtained are in line with the existence of two paired helix-loop-helix (HLH) motifs.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19546223 F.Schumann, H.Hoffmeister, R.Bader, M.Schmidt, R.Witzgall, and H.R.Kalbitzer (2009).
Ca2+-dependent conformational changes in a C-terminal cytosolic domain of polycystin-2.
  J Biol Chem, 284, 24372-24383.  
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