Schreier, Christina and Auer, Alexandra and Kalbitzer, Hans Robert and Kremer, Werner (2009) NMR assignments of a 48 kDa tetramer of the T1 domain of the mammalian voltage gated potassium channel Kv1.4. BIOMOLECULAR NMR ASSIGNMENTS, 3 (2). pp. 167-170. ISSN 1874-2718, 1874-270X
Full text not available from this repository. (Request a copy)Abstract
The N-terminal cytosolic T1 domain of the mammalian voltage gated potassium channel Kv1.4 is strongly involved in the tetramerization of the Kv1.4 subunit that is required for forming a functional ion channel. The T1 domain forms a stable tetramer of 48 kDa in solution that cannot be dissociated into monomers. In spite of the high molecular mass it was possible to completely assign the backbone and part of the side chain resonances by multidimensional NMR spectroscopy on uniformly H-2, C-13, N-15 enriched protein. The secondary structure analysis derived from the chemical shifts is in line with the expectations from X-ray structures of related proteins.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | INACTIVATION; C-13; Voltage gated potassium channel; NMR resonance assignments; T1 Domain |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 27 Aug 2020 12:21 |
| Last Modified: | 27 Aug 2020 12:21 |
| URI: | https://pred.uni-regensburg.de/id/eprint/28002 |
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