User:Ralf Stephan/Sandbox 2: Difference between revisions
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TCDB, the most sophisticated classification of transport proteins to date, classify ion channels as a heterogenous subset of all '''α-type channels''', whose singular property is to consist mainly of [[alpha helix|α-helices]] that span the membrane. They are distinct in this from the [[beta-barrel porins]], but also from non-ribosomally synthesized channels like [[gramicidin]], [[polyglutamine]] or [[digitoxin]]. All these proteins are '''passive''' transport proteins. | TCDB, the most sophisticated classification of transport proteins to date, classify ion channels as a heterogenous subset of all '''α-type channels''', whose singular property is to consist mainly of [[alpha helix|α-helices]] that span the membrane. They are distinct in this from the [[beta-barrel porins]], but also from non-ribosomally synthesized channels like [[gramicidin]], [[polyglutamine]] or [[digitoxin]]. All these proteins are '''passive''' transport proteins. | ||
== Available structures == | |||
Membrane transport proteins are notoriously difficult to crystallize while in a working state. So, it's no surprise that there are preciously few structure data for ion channels. At the moment, the following ion channels have been at least partly resolved: | |||
* the [[voltage-gated passium channel]] from ''Streptomyces lividans'' with the structures [[1bl8]], [[1k4c]], [[1k4d]] | |||
* the [[calcium-gated potassium channel mthK]] from ''Methanobacterium thermoautotrophicum'' ([[1lnq]]) | |||
* the [[voltage-gated potassium channel]] K<sub>v</sub>AP from ''Aeropyrum pernix'' ([[1onq]]) | |||
* a [[potassium channel]] from ''Burkholderia pseudomallei'' ([[1p7b]]) | |||
* [[aquaporins]] from several species: | |||
** ''Methanobacterium thermoautotrophicum'' (aqpM, [[2evu]], [[2f2c]]) | |||
** ''E. coli'' K12 (Aquaporin Z, [[1r2c]], [[2abm]]) | |||
** the [[glycerol uptake facilitator]] from ''E. coli'' K12 ([[1fx8]]) | |||
** ''Homo sapiens'' (AQP-1, [[1fqy]], [[1ih5]]) | |||
** ''Bos taurus'' (Aquaporin-0, [[1ymg]], [[2b6p]]) | |||
* the [[ammonia transporter]] from ''E. coli'' K12 ([[1u7g]], [[1xqf]], [[2ns1]], [[2nuu]]) | |||
* the [[ammonium transporter]] from ''Archaeoglobus fulgidus'' ([[2b2f]]) | |||
* the small-conductance [[mechanosensitive channel]] from ''E. coli'' K12 ([[2oau]]) | |||
* human [[phospholamban]] ([[1zll]]) | |||
== Weblinks == | == Weblinks == | ||
*[http://www.tcdb.org/ The TCDB database] | *[http://www.tcdb.org/ The TCDB database] | ||
*[http://www.tcdb.org/tcdb/subclass2.php?tc=1.A TCDB: 1.A α-Type channels] | *[http://www.tcdb.org/tcdb/subclass2.php?tc=1.A TCDB: 1.A α-Type channels] | ||
*[http://www.tcdb.org/pdb_structure.php TCDB: Transport proteins with PDB structures] | *[http://www.tcdb.org/pdb_structure.php TCDB: Transport proteins with PDB structures] |
Revision as of 12:24, 13 February 2009
Ion channels are membrane proteins that catalyze the passive transport of ions through the cell membrane. Most ion channels are specific to an ion, like the natrium channels, or the chloride channels. Some, like the TRP channels, let through a bunch of cations. Another property of ion channels is that they can be either driven by voltage or concentration gradients, or they can be gated (by voltage, ligands, touch and other sensory signal). Finally, ion channels are the fastest of all membrane transporters, with 10^6 to 10^8 transported units per second versus 10^2 to 10^4 molecules per second for porters/carriers, or 10^0 to 10^3 for ATP-driven pumps.
ClassificationClassification
TCDB, the most sophisticated classification of transport proteins to date, classify ion channels as a heterogenous subset of all α-type channels, whose singular property is to consist mainly of α-helices that span the membrane. They are distinct in this from the beta-barrel porins, but also from non-ribosomally synthesized channels like gramicidin, polyglutamine or digitoxin. All these proteins are passive transport proteins.
Available structuresAvailable structures
Membrane transport proteins are notoriously difficult to crystallize while in a working state. So, it's no surprise that there are preciously few structure data for ion channels. At the moment, the following ion channels have been at least partly resolved:
- the voltage-gated passium channel from Streptomyces lividans with the structures 1bl8, 1k4c, 1k4d
- the calcium-gated potassium channel mthK from Methanobacterium thermoautotrophicum (1lnq)
- the voltage-gated potassium channel KvAP from Aeropyrum pernix (1onq)
- a potassium channel from Burkholderia pseudomallei (1p7b)
- aquaporins from several species:
- the ammonia transporter from E. coli K12 (1u7g, 1xqf, 2ns1, 2nuu)
- the ammonium transporter from Archaeoglobus fulgidus (2b2f)
- the small-conductance mechanosensitive channel from E. coli K12 (2oau)
- human phospholamban (1zll)