1T1D
CRYSTAL STRUCTURE OF THE TETRAMERIZATION DOMAIN OF THE SHAKER POTASSIUM CHANNEL
Summary for 1T1D
| Entry DOI | 10.2210/pdb1t1d/pdb |
| Descriptor | PROTEIN (POTASSIUM CHANNEL KV1.1) (2 entities in total) |
| Functional Keywords | potassium channels, tetramerization domain, aplysia kv1.1, proton transport, membrane protein |
| Biological source | Aplysia californica (California sea hare) |
| Total number of polymer chains | 1 |
| Total formula weight | 12097.45 |
| Authors | Kreusch, A.,Pfaffinger, P.J.,Stevens, C.F.,Choe, S. (deposition date: 1998-09-22, release date: 1999-01-13, Last modification date: 2023-08-23) |
| Primary citation | Bixby, K.A.,Nanao, M.H.,Shen, N.V.,Kreusch, A.,Bellamy, H.,Pfaffinger, P.J.,Choe, S. Zn2+-binding and molecular determinants of tetramerization in voltage-gated K+ channels. Nat.Struct.Biol., 6:38-43, 1999 Cited by PubMed Abstract: The N-terminal, cytoplasmic tetramerization domain (T1) of voltage-gated K+ channels encodes molecular determinants for subfamily-specific assembly of alpha-subunits into functional tetrameric channels. Crystal structures of T1 tetramers from Shaw and Shaker subfamilies reveal a common four-layered scaffolding. Within layer 4, on the hypothetical membrane-facing side of the tetramer, the Shaw T1 tetramer contains four zinc ions; each is coordinated by a histidine and two cysteines from one monomer and by one cysteine from an adjacent monomer. The amino acids involved in coordinating the Zn2+ ion occur in a HX5CX20CC sequence motif that is highly conserved among all Shab, Shaw and Shal subfamily members, but is not found in Shaker subfamily members. We demonstrate by coimmunoprecipitation that a few characteristic residues in the subunit interface are crucial for subfamily-specific tetramerization of the T1 domains. PubMed: 9886290DOI: 10.1038/4911 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
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