User:Ralf Stephan/Sandbox 2: Difference between revisions
Ralf Stephan (talk | contribs) available structures |
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== Available structures == | == 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: | 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 α-type ion channels have been at least partly resolved: | ||
* the [[voltage-gated | * the [[voltage-dependent potassium channel]] from ''Rattus norvegicus'' ([[1exb]]) | ||
* the [[voltage-gated potassium channel]] from ''Streptomyces lividans'' with the structures [[1bl8]], [[1k4c]], [[1k4d]] | |||
* the [[calcium-gated potassium channel mthK]] from ''Methanobacterium thermoautotrophicum'' ([[1lnq]]) | * the [[calcium-gated potassium channel mthK]] from ''Methanobacterium thermoautotrophicum'' ([[1lnq]]) | ||
* the [[voltage-gated potassium channel]] K<sub>v</sub>AP from ''Aeropyrum pernix'' ([[1onq]]) | * the [[voltage-gated potassium channel]] K<sub>v</sub>AP from ''Aeropyrum pernix'' ([[1onq]]) | ||
* the [[voltage-gated calcium channel]] Ca<sub>V</sub> ([[1toh]], [[1toj]]) | |||
* the hyperpolarization-activated and cyclic nucleotide-gated K+ channel [[HCN]] from ''Mus musculus'' ([[1q3e]], [[1q43]], [[1q5o]]) | |||
* the [[Inward Rectifier Potassium Channel]] KirBac3.1 ([[1xl4]],[[1xl6]]) | |||
* receptor channels like | |||
** the [[nicotinic acetylcholine-activated cation-selective channel]] from ''Torpedo marmorata'' ([[1oed]]) | |||
** the [[glutamate receptor]] 2 | |||
* a [[potassium channel]] from ''Burkholderia pseudomallei'' ([[1p7b]]) | * a [[potassium channel]] from ''Burkholderia pseudomallei'' ([[1p7b]]) | ||
* the [[ammonium transporter]] from ''Archaeoglobus fulgidus'' ([[2b2f]]) | * the [[ammonium transporter]] from ''Archaeoglobus fulgidus'' ([[2b2f]]) | ||
* the small-conductance [[mechanosensitive channel]] from ''E. coli'' K12 ([[2oau]]) | * the small-conductance [[mechanosensitive channel]] from ''E. coli'' K12 ([[2oau]]) | ||
* human [[phospholamban]] ([[1zll]]) | * human [[phospholamban]] ([[1zll]]) | ||
* the P7 [[viroporin]] of Hepatitis C virus ([[2k8j]]) | |||
Additionally the following non-ribosomally synthesized channel proteins constitute ion channels, and have their structure resolved: | |||
* [[Gramicidin]] ([[1av2]], [[1c4d]], [[1mag]]) | |||
* fungal [[Antiamoebin]] ([[1joh]], [[1gq0]]) | |||
* fungal [[Trichotoxin]] ([[1m24]]) | |||
* further [[Peptaibol]] antibiotics ([[1ob4]], [[1ob6]], [[1ob7]]) | |||
We do not count ClC chloride carriers as ion channels, as they are secondary active [[carriers]]. | |||
== 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 13:27, 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 α-type ion channels have been at least partly resolved:
- the voltage-dependent potassium channel from Rattus norvegicus (1exb)
- the voltage-gated potassium 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)
- the voltage-gated calcium channel CaV (1toh, 1toj)
- the hyperpolarization-activated and cyclic nucleotide-gated K+ channel HCN from Mus musculus (1q3e, 1q43, 1q5o)
- the Inward Rectifier Potassium Channel KirBac3.1 (1xl4,1xl6)
- receptor channels like
- the nicotinic acetylcholine-activated cation-selective channel from Torpedo marmorata (1oed)
- the glutamate receptor 2
- a potassium channel from Burkholderia pseudomallei (1p7b)
- the ammonium transporter from Archaeoglobus fulgidus (2b2f)
- the small-conductance mechanosensitive channel from E. coli K12 (2oau)
- human phospholamban (1zll)
- the P7 viroporin of Hepatitis C virus (2k8j)
Additionally the following non-ribosomally synthesized channel proteins constitute ion channels, and have their structure resolved:
- Gramicidin (1av2, 1c4d, 1mag)
- fungal Antiamoebin (1joh, 1gq0)
- fungal Trichotoxin (1m24)
- further Peptaibol antibiotics (1ob4, 1ob6, 1ob7)
We do not count ClC chloride carriers as ion channels, as they are secondary active carriers.