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1j95
From Proteopedia
| 1j95, resolution 2.80Å () | |||||||||
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| Ligands: | , | ||||||||
| Domains: | Ion_trans_2 | ||||||||
| Related: | 1bl8 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
KCSA potassium channel with TBA (tetrabutylammonium) and potassium
Many voltage-dependent K+ channels open when the membrane is depolarized and then rapidly close by a process called inactivation. Neurons use inactivating K+ channels to modulate their firing frequency. In Shaker-type K+ channels, the inactivation gate, which is responsible for the closing of the channel, is formed by the channel's cytoplasmic amino terminus. Here we show that the central cavity and inner pore of the K+ channel form the receptor site for both the inactivation gate and small-molecule inhibitors. We propose that inactivation occurs by a sequential reaction in which the gate binds initially to the cytoplasmic channel surface and then enters the pore as an extended peptide. This mechanism accounts for the functional properties of K+ channel inactivation and indicates that the cavity may be the site of action for certain drugs that alter cation channel function.
Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors., Zhou M, Morais-Cabral JH, Mann S, MacKinnon R, Nature. 2001 Jun 7;411(6838):657-61. PMID:11395760
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1J95 is a 4 chains structure of sequences from Streptomyces lividans. Full crystallographic information is available from OCA.
Reference
- Zhou M, Morais-Cabral JH, Mann S, MacKinnon R. Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature. 2001 Jun 7;411(6838):657-61. PMID:11395760 doi:10.1038/35079500
Page seeded by OCA on Tue Feb 17 12:00:20 2009
