期刊
NEURON
卷 29, 期 3, 页码 593-601出版社
CELL PRESS
DOI: 10.1016/S0896-6273(01)00236-7
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资金
- NCRR NIH HHS [RR00862] Funding Source: Medline
- PHS HHS [47400] Funding Source: Medline
The intracellular C-terminal domain structure of a six-transmembrane K+ channel from Escherichia coli has been solved by X-ray crystallography at 2.4 Angstrom resolution. The structure is representative of a broad class of domains/proteins that regulate the conductance of K+ there referred to as RCK domains) in prokaryotic K+ transporters and K+ channels. The RCK domain has a Rossmann-fold topology with unique positions, not commonly conserved among Rossmann-fold proteins, composing a well-conserved salt bridge and a hydrophobic dimer interface. Structure-based amino acid sequence alignments and mutational analysis are used to demonstrate that an RCK domain is also present and is an important component of the gating machinery in eukaryotic large-conductance Ca2+-activated K+ channels.
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