3KVT

TETRAMERIZATION DOMAIN FROM AKV3.1 (SHAW-SUBFAMILY) VOLTAGE-GATED POTASSIUM CHANNEL

Summary for 3KVT

• Entry DOI: 10.2210/pdb3kvt/pdb
• Descriptor: POTASSIUM CHANNEL PROTEIN SHAW, ZINC ION (3 entities in total)
• Functional Keywords: potassium channel, tetramerization domain, molecular recognition, zinc-binding
• Biological source: Aplysia californica (California sea hare)
• Total number of polymer chains: 1
• Total formula weight: 13454.56

Authors

Bixby, K.A.,Nanao, M.H.,Shen, N.V.,Kreusch, A.,Bellamy, H.,Pfaffinger, P.J.,Choe, S. (deposition date: 1998-09-25, release date: 1999-01-13, Last modification date: 2024-04-03)

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

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: 9886290
DOI: 10.1038/4911

Experimental method

X-RAY DIFFRACTION (2 Å)