1j95
From Proteopedia
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| - | [[Image:1j95.jpg|left|200px]] | + | [[Image:1j95.jpg|left|200px]] |
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| - | '''KCSA potassium channel with TBA (tetrabutylammonium) and potassium''' | + | {{Structure |
| + | |PDB= 1j95 |SIZE=350|CAPTION= <scene name='initialview01'>1j95</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=TBA:TETRABUTYLAMMONIUM ION'>TBA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''KCSA potassium channel with TBA (tetrabutylammonium) and potassium''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1J95 is a [ | + | 1J95 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J95 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11395760 11395760] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces lividans]] | [[Category: Streptomyces lividans]] | ||
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[[Category: metal transport]] | [[Category: metal transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:00:13 2008'' |
Revision as of 10:00, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
KCSA potassium channel with TBA (tetrabutylammonium) and potassium
Overview
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.
About this Structure
1J95 is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 12:00:13 2008
