Schumann, Frank and Hoffmeister, Helen and Bader, Reto and Schmidt, Maren and Witzgall, Ralph and Kalbitzer, Hans Robert (2009) Ca2(+)-dependent Conformational Changes in a C-terminal Cytosolic Domain of Polycystin-2. JOURNAL OF BIOLOGICAL CHEMISTRY, 284 (36). pp. 24372-24383. ISSN 0021-9258, 1083-351X
Full text not available from this repository. (Request a copy)Abstract
The PKD1 and PKD2 genes are the genes that are mutated in patients suffering from autosomal dominant polycystic kidney disease. The human PKD2 gene codes for a968-amino acid long membrane protein called polycystin-2 that represents a cation channel whose activity can be regulated by Ca2+ ions. By CD, fluorescence, and NMR spectroscopy, we have studied a 117-amino acid-long fragment of the cytoplasmic domain of polycystin-2, polycystin-2-(680-796) that was proposed to contain a Ca2+-binding site. NMR structure determination reveals the existence of two Ca2+-binding sites in polycystin-2-(680-796) arranged in a typical and an a typical EF-hand motif. In the absence of Ca2+ the protein forms a dimer that is dissociated by Ca2+ binding. This dissociation may be related to the Ca2+ inactivation observed earlier. The calcium affinity of the protein was determined by fluorescence and NMR spectroscopy. At 293 K, the K-D values for the high and low affinity sites are 55 mu M and 179 mu M, respectively.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SOLUTION NMR STRUCTURES; KIDNEY-DISEASE; CHEMICAL-SHIFT; CATION CHANNEL; PROTEIN; SPECTROSCOPY; DATABASE; SOLVENT; SERVER; ACID; |
| 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: | 07 Sep 2020 08:26 |
| Last Modified: | 07 Sep 2020 08:26 |
| URI: | https://pred.uni-regensburg.de/id/eprint/28417 |
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