Abstract：
: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 A resolution. The structure is representative of a broad class of domains/proteins that regulate the conductance of K+ (here 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.
journal_name
Neuronjournal_title
Neuronauthors
Jiang Y,Pico A,Cadene M,Chait BT,MacKinnon Rdoi
10.1016/s0896-6273(01)00236-7subject
Has Abstractpub_date
2001-03-01 00:00:00pages
593-601issue
3eissn
0896-6273issn
1097-4199pii
S0896-6273(01)00236-7journal_volume
29pub_type
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