Ion channels
From Proteopedia
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+ | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
- | + | * Potassium channel See: [[Potassium_Channel#Additional_Structures_of_Potassium_Channels|Potassium Channels]] | |
- | + | * Calcium channel | |
- | + | **[[3bxx]] – rCav2.1 α 1A subunit+calmodulin<br /> | |
+ | **[[3bxl]] - rCav2.3 α 1E subunit+calmodulin<br /> | ||
+ | **[[2f3y]], [[2f3z]], [[2be6]] – hCav1.2 α 1C subunit+calmodulin<br /> | ||
+ | **[[1t0h]] – rVDCC β 2A subunit <br /> | ||
+ | **[[1t0j]] – rVDCC β 2A+α 1C <br /> | ||
+ | **[[1vyt]] - rVDCC β 3+α 1C <br /> | ||
+ | **[[1vyu]] – rVDCC β 3<br /> | ||
+ | **[[1vyv]] - rVDCC β 4<br /> | ||
+ | **[[1t3l]] - raVDCC β 2+α 1S – rabbit<br /> | ||
+ | **[[1t3s]] - raVDCC β 2<br /> | ||
+ | **[[2d46]] – hVDCC β 4a – NMR<br /> | ||
+ | **[[3dve]], [[3dvj]], [[3dvk]], [[3dvm]], [[3g43]] - rCav2.2 α 1B subunit+hCalmodulin<br /> | ||
+ | **[[3oxq]] - hCav2.1 α 1C subunit IQ domain+hCalmodulin<br /> | ||
+ | **[[2vay]], [[3oxq]] - hCav1.1 α 1S subunit IQ domain+hCalmodulin<br /> | ||
+ | **[[1hvd]], [[1hve]], [[1hvf]], [[1hvg]] – hAnnexin V (mutant) | ||
- | + | *Sodium channel | |
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- | + | **[[1byy]] - rNaCh IIA inactivation fragment<br /> | |
+ | **[[2kav]], [[2kbi]] - hNaCh IIA C-terminal EF-hand domain - NMR | ||
- | + | * NH4+ channel | |
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- | + | **[[2nmr]], [[2nop]], [[2now]], [[2npc]], [[2npd]], [[2npe]], [[2npj]], [[2npg]], [[2npk]], [[1u77]], [[1u7c]], [[1u7g]], [[1xqe]], [[1xqf]] – EcAmCh – ''Escherichia coli''<br /> | |
+ | **[[2b2h]], [[2b2i]], [[2b2j]], [[2b2f]] – AmCh – ''Archaeglobus fulgidus''<br /> | ||
+ | **[[3b9w]], [[3b9y]], [[3bhs]] – AmCh – ''Nitrosomonas europaea'' | ||
- | + | * MscL and MscS | |
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- | + | **[[3hzq]] – MscL – ''Staphylococcus aureus''<br /> | |
+ | **[[2oar]] – MscL – ''Mycobacterium tuberculosis''<br /> | ||
+ | **[[2oau]], [[2vv5]] - EcMscS | ||
- | + | * Chloride channel | |
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- | + | **[[1rk4]], [[3swl]] - hClCh protein 1<br /> | |
+ | **[[3o3t]], [[3p8w]], [[3p90]], [[1k0o]], [[3qr6]], [[3tgz]] - hClCh protein 1 (mutant)<br /> | ||
+ | **[[2per]], [[2r4v]], [[2r5g]] - hClCh protein 2<br /> | ||
+ | **[[3kjy]], [[3fy7]] - hClCh protein 3 residues 1-230<br /> | ||
+ | **[[2ahe]], [[2d2z]] – hClCh protein 4<br /> | ||
- | + | * Anion Channel (Outer mitochondrial membrane protein porin 1) | |
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- | + | **[[2jk4]], [[2k4t]] – hVDAC<br /> | |
+ | **[[3emn]] – mVDAC - mouse<br /> | ||
- | + | * Ligand-gated ion channel | |
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- | + | **[[2vl0]] – EcLGIC – ''Erwinia chrysanthemi''<br /> | |
+ | **[[2yks]] - EcLGIC (mutant)<br /> | ||
+ | **[[2xq3]], [[2xq4]], [[2xq5]], [[2xq6]], [[2xq7]], [[2xqa]], [[2xq8]] – GvLGIC+inhibitor – ''Gloeobacter violaceus''<br /> | ||
+ | **[[3eam]], [[3ehz]] – GvLGIC<br /> | ||
+ | **[[3igq]] – GvLGIC N-terminal<br /> | ||
+ | **[[2xq9]] – GvLGIC (mutant)+inhibitor<br /> | ||
+ | **[[3p4w]], [[3p50]] – GvLGIC + general anaesthetic<br /> | ||
+ | **[[3lsv]], [[3tls]], [[3tlt]], [[3tlu]], [[3tlv]], [[3tlw]], [[3uu3]], [[3uu4]], [[3uu5]], [[3uu6]], [[3uu8]], [[3uub]] – GvLGIC (mutant)<br /> | ||
+ | **[[4f8h]] – GvLGIC + ketamine<br /> | ||
+ | **[[4a97]], [[4a98]] – EcElic + benzodiazepine | ||
- | + | * Cyclic Nucleotide-Gated channel | |
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- | + | **[[3etq]], [[3ffq]], [[3u0z]], [[3u10]], [[3u11]] - mCNGC C-terminal<br /> | |
+ | **[[1q3e]], [[1q43]], [[1q5o]] - mCNGC 2 fragment + nucleotide<br /> | ||
+ | **[[2q0a]] - mCNGC 2 C-terminal (mutant)<br /> | ||
+ | **[[3bpz]] - mCNGC 2 ligand-binding domain <br /> | ||
+ | **[[2zd9]], [[3beh]] - MlCNGC<br /> | ||
+ | **[[4chv]], [[4chw]] – MlCNGC – Cryo EM<br /> | ||
+ | **[[2ptm]] - CNGC C-terminal - ''Strongylocentratus purpuratus''<br /> | ||
+ | **[[3co2]] - MlCNGC ligand-binding domain (mutant) – ''Mesorhizobium loti''<br /> | ||
+ | **[[2kxl]] - ligand-binding domain – NMR<br /> | ||
+ | **[[3beh]] - MlCNGC<br /> | ||
+ | **[[3otf]] – hCNGC 4 ligand-binding domain<br /> | ||
+ | **[[4hbn]] – hCNGC 4 ligand-binding domain (mutant)<br /> | ||
+ | **[[4nvp]] – hCNGC 4 ligand-binding domain + 7-CH-cAMP<br /> | ||
- | + | * Acid sensitive ion channel | |
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- | + | **[[3hgc]], [[3ij4]], [[2qts]], [[3s3w]] – cASC – chicken<br /> | |
+ | **[[3s3x]], [[4fz0]], [[4fz1]] – cASC + psalmotoxin | ||
- | + | * ATP-Gated channel (AGC) | |
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- | + | **[[3h9v]], [[3i5d]] – AGC – Zebra fish | |
- | + | * Proton channel | |
- | + | **[[2kih]], [[2kwx]] – IVproton channel – Influenza virus<br /> | |
+ | **[[2rtf]] - IVproton channel + inhibitor - NMR<br /> | ||
+ | **[[3c9j]] - IVproton channel transmembrane domain + inhibitor<br /> | ||
+ | **[[3bkd]] - IVproton channel transmembrane domain<br /> | ||
+ | **[[1nyj]], [[1mp6]] - IVproton channel transmembrane domain - NMR<br /> | ||
+ | **[[2kj1]], [[2l0j]] - IVproton channel – NMR | ||
- | + | * Voltage-gated hydrogen channel (VGHC) | |
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- | [[3a2a]] – hVGHC C-terminal - NMR <br /> | + | **[[3a2a]] – hVGHC C-terminal - NMR <br /> |
- | [[3vmx]] – mVGHC C-terminal | + | **[[3vmx]] – mVGHC C-terminal |
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- | + | *Nicotinic acetylcholine receptor | |
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- | + | **[[1oed]], [[2bg9]], [[4bor]] - AChR - ''Torpeco marmorata'' - EM<br /> | |
+ | **[[2k58]] - AChR β2 subunit 1st transmembrane domain - NMR<br /> | ||
+ | **[[2k59]] - AChR β2 subunit - NMR | ||
- | + | *Tryptophan channel | |
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- | + | **[[2rfa]] - mTrpCh ankyrin repeat domain<br /> | |
+ | **[[3e7k]] - rTrpCh tetramerization domain | ||
- | + | *Glycerol facilitator | |
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+ | **[[1lda]], [[1ldi]] - EcGlpF<br /> | ||
+ | **[[1fx8]] - EcGlpF + glycerol<br /> | ||
+ | **[[1ldf]] - EcGlpF (mutant) | ||
+ | }} | ||
== Weblinks == | == Weblinks == | ||
*[http://www.tcdb.org/ The TCDB database] | *[http://www.tcdb.org/ The TCDB database] |
Revision as of 07:49, 30 November 2014
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 sodium channels, or the chloride channels. Some, like the TRP channels, let through various 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). Potassium channels (KCh) are subdivided to voltage-gated KCh and calcium-dependent KCh. The latter are subdivided into high- (BK, LKCa), intermediate- and small-conductance KCh (human SK1, rat SK2, SKCa).
MthK is a calcium-dependent potassium channel from Methanobacterium thermoautrophicum. MscL and MscS are large- and small-conductance mechanosensitive channels which protect bacteria from osmotic shock by allowing ions to flow across the cell membrane Mechanosensitive channels: opening and closing. Voltage-Dependent Calcium Channels (VDCC) allow Ca++ to enter the cell resulting in muscle contraction, neuron excitation or hormone release. VDCC are composed of several subunits and are named as a Cav gene product. Finally, ion channels are the fastest of all membrane transporters, with 106 to 108 transported units per second versus 102 to 104 molecules per second for porters/carriers, or 100 to 103 for ATP-driven pumps. The images at the left and at the right correspond to one representative ion channel structure, i.e. the crystal structure of voltage-dependent potassium channel from Rattus norvegicus (1qrq). Specific details in:
- Proton Channels,
- Membrane Channels & Pumps,
- M2 Proton Channel,
- M2 Proton Channel Inhibitor Pharmacokinetics,
- User:Michael Strong/H1N1/MP give details on proton channels,
- User:Michael Strong/H1N1/MP1/MSA,
- User:Michael Strong/H1N1/MP2/MSA for multiple sequence alignment
- Chloride Ion Channel
- User:Laura Fountain/Chloride Ion Channel
- Chloride Intracellular Channel Protein 2
- Mechanosensitive channels: opening and closing
- Voltage-gated calcium channels.
Contents |
Classification
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 and the pore-forming toxins, as well as from non-ribosomally synthesized channels like gramicidin, polyglutamine or digitoxin. All these proteins are passive transport proteins.
Additional Resources
For additional information, see: Membrane Channels & Pumps
For additional information, see: Hypertension & Congestive Heart Failure
Available 3D structures
Ion channels translate ionic fluxes across cell membrane into electrical impulses. MscL and MscS are large- and small-conductance mechanosensitive channels which protect bacteria from osmotic shock by allowing ions to flow across the cell membrane. Voltage-Dependent Calcium Channels (VDCC) allow Ca to enter the cell resulting in muscle contraction, neuron excitation or hormone release. VDCC are composed of several subunits and are named as a Cav gene product. The human annexin V molecule serves as a calcium channel. There are also Voltage-Dependent Anion Channels (VDAC). Chloride ion channels (ClCh) are involved in maintaining pH, volume homeostasis and more. Ligand-Gated Ion Channels (LGIC) open or close when binding a ligand like a neurotransmitter. The Cyclic Nucleotide-Gated channel (CNGC) conduct cations upon binding of cAMP or cGMP. The Acid-Sensitive channels (ASC) conduct cations upon binding of acid. The glycerol facilitator (GlpF) is a protein channel which transports glycerol across the cell membrane of E. coli. Other ion channel proteins are the aquaporins, gramicidin, antiamoebin, trichotoxin, peptaibol and the glutamate receptor.
Updated on 30-November-2014
Weblinks
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Wayne Decatur, David Canner, Eric Martz, Ralf Stephan, Jaime Prilusky, Ilan Samish, Shelly Livne