2KLE

ISIC Refined Solution Structure of the Calcium Binding Domain of the C-terminal Cytosolic Domain of Polycystin-2

Summary for 2KLE

• Entry DOI: 10.2210/pdb2kle/pdb
• Related: 2KLD
• NMR Information: BMRB: 16191
• Descriptor: Polycystin-2 (1 entity in total)
• Functional Keywords: pc2, pkd2, calcium binding domain, ef hand, cytosolic, calcium, coiled coil, disease mutation, glycoprotein, ion transport, ionic channel, membrane, phosphoprotein, polymorphism, transmembrane, transport, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Multi-pass membrane protein (Potential): Q13563
• Total number of polymer chains: 1
• Total formula weight: 14024.42

Authors

Kalbitzer, H.R. (deposition date: 2009-07-01, release date: 2009-07-28, Last modification date: 2024-05-29)

Primary citation

Schumann, F.H.,Hoffmeister, H.,Schmidt, M.,Bader, R.,Besl, E.,Witzgall, R.,Kalbitzer, H.R.
NMR-assignments of a cytosolic domain of the C-terminus of polycystin-2
Biomol.Nmr Assign., 3:141-144, 2009

PubMed Abstract: 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.

PubMed: 19636966
DOI: 10.1007/s12104-009-9160-x

Experimental method

SOLUTION NMR