title: NMR assignments of a 48 kDa tetramer of the T1 domain of the mammalian voltage gated potassium channel Kv1.4.
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 (2)H, (13)C, (15)N enriched protein. The secondary structure analysis derived from the chemical shifts is in line with the expectations from X-ray structures of related proteins.
authors.affiliation: Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040, Regensburg, Germany.
authors.forename: Christina
authors.initials: C
authors.lastname: Schreier
authors.forename: Alexandra
authors.initials: A
authors.lastname: Auer
authors.forename: Hans Robert
authors.initials: HR
authors.lastname: Kalbitzer
authors.forename: Werner
authors.initials: W
authors.lastname: Kremer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D051665:Kv1.4 Potassium Channel / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019906:Nuclear Magnetic Resonance, Biomolecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D051381:Rats
chemical_list: D051665:Kv1.4 Potassium Channel