Schumann, Frank H. and Hoffmeister, Helen and Schmidt, Maren and Bader, Reto and Besl, Elisabeth and Witzgall, Ralph and Kalbitzer, Hans Robert (2009) NMR-assignments of a cytosolic domain of the C-terminus of polycystin-2. BIOMOLECULAR NMR ASSIGNMENTS, 3 (1). pp. 141-144. ISSN 1874-2718, 1874-270X
Full text not available from this repository. (Request a copy)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 C-13 and N-15. 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEINS; Polycystin-2; PKD2; Polycystic kidney disease; NMR structure; EF-hand |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer Biology, Preclinical Medicine > Institut für Anatomie > Lehrstuhl für Molekulare und zelluläre Anatomie > Prof. Dr. Ralph Witzgall |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Sep 2020 08:56 |
| Last Modified: | 14 Sep 2020 08:56 |
| URI: | https://pred.uni-regensburg.de/id/eprint/28844 |
Actions (login required)
 |
View Item |
