User:Lori Wetmore/Sandbox 3
From Proteopedia
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Each pore contains a <scene name='User:Lori_Wetmore/Sandbox_3/Selectivity_filter_1/1'>selectivity filter</scene> that connects the intracellular and extracellular aqueous environments. The allows Cl- ions through the channel, while keeping out ____. The chloride ion interacts with the side chains of the Ser107 and Tyr445 residues (yellow). | Each pore contains a <scene name='User:Lori_Wetmore/Sandbox_3/Selectivity_filter_1/1'>selectivity filter</scene> that connects the intracellular and extracellular aqueous environments. The allows Cl- ions through the channel, while keeping out ____. The chloride ion interacts with the side chains of the Ser107 and Tyr445 residues (yellow). | ||
| + | <br> | ||
<scene name='User:Lori_Wetmore/Sandbox_3/Orange_top/1'>Orange Top</scene><br> | <scene name='User:Lori_Wetmore/Sandbox_3/Orange_top/1'>Orange Top</scene><br> | ||
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==ClC-0== | ==ClC-0== | ||
| - | In order to study the selectivity filter of the ClC channels, a complex was created between the ClC channel from ____ and a Fab antibody [??] | + | In order to study the selectivity filter of the ClC channels, a complex was created between the ClC channel from ____ and a Fab antibody [??]<br> |
| + | |||
| + | The chloride channel consists of three possible binding sites for the chloride ion. These binding sites are known as S<subscript>int</subscript>, S<subscript>cen</subscript>, and S<subscript>ext</subscript>. | ||
| + | |||
| + | The ClC-0 [others too?] channel has been shown to be gated by the Glu148 residue. When the Glu148 residue is in the "off" conformation, it blocks the | ||
Revision as of 02:25, 29 September 2010
Contents |
Chloride Channels
Chloride channels come in many varieties.
ClC Channels
The ClC family of chloride channels are present in many species. Mammals contain 9 different types of ClC channels[1]. The members of the CLC channel family can be divided into different groups by a number of different characteristics including intracellular localization, tissue [specificity?], and basic function [2].
| ClC Channels within Homo sapiens | |||
|---|---|---|---|
| Channel Name | Tissue | Location Within Cell | Basic Function |
| ClC-1 | Skeletal Muscle | Plasma Membrane Ion Channel | |
| ClC-2 | Plasma Membrane Ion Channel | ||
| ClC-3 | H+/Cl- Exchange Transporter | ||
| ClC-4 | H+/Cl- Exchange Transporter | ||
| ClC-5 | H+/Cl- Exchange Transporter | ||
| ClC-6 | |||
| ClC-7 | |||
| ClC-Ka | Plasma Membrane Ion Channel | ||
| ClC-Kb | Plasma Membrane Ion Channel | ||
The Structure of ClC Channels
|
Though the basic types and functions of several ClC channels within eukaryotes have been elucidated, no exact structural information exists for eukaryotic ClC channels. Therefore, much of the current knowledge regarding ClC channel structure has come from the elucidation of the ClC structures of prokaryotes such as E. coli[3] and S. typhimurium[4].
The ClC channel is composed of two subunits, with each subunit consisting of 18 alpha helices. The two subunits form a dimer, and there is an extensive interface between the two subunits. However, the interaction between the two dimers is not necessary for pore formation[5].Instead, the basic structure of ClC channels is that of a , in which each of the subunits contains its own pore, and two subunit monomers combine to form a double-pore channel [6]. Within ClC-0, the two . This double-barreled structure applies particularly to the ___ channels. Each of these pores is capable of transporting Cl- ions (light blue).
Each pore contains a that connects the intracellular and extracellular aqueous environments. The allows Cl- ions through the channel, while keeping out ____. The chloride ion interacts with the side chains of the Ser107 and Tyr445 residues (yellow).
<<<<---this one's wrong
<<<<---so is this one
<<<<<<-----change this so that you can see it better
ClC-0
In order to study the selectivity filter of the ClC channels, a complex was created between the ClC channel from ____ and a Fab antibody [??]
The chloride channel consists of three possible binding sites for the chloride ion. These binding sites are known as S<subscript>int</subscript>, S<subscript>cen</subscript>, and S<subscript>ext</subscript>.
The ClC-0 [others too?] channel has been shown to be gated by the Glu148 residue. When the Glu148 residue is in the "off" conformation, it blocks the
two repeated units talked about here ((http://www.nature.com/nature/journal/v415/n6869/fig_tab/415276a_F2.html))
1ots 2h2p 1kpl
Other Notes and Things
RAINBOW TIME
When viewed in (where the N-terminus is gradually shaded into the C-terminus according to the scale below)
| N | C |
References
- ↑ Jentsch TJ, Stein V, Weinreich F, Zdebik AA. Molecular structure and physiological function of chloride channels. Physiol Rev. 2002 Apr;82(2):503-68. PMID:11917096 doi:10.1152/physrev.00029.2001
- ↑ Accardi A, Walden M, Nguitragool W, Jayaram H, Williams C, Miller C. Separate ion pathways in a Cl-/H+ exchanger. J Gen Physiol. 2005 Dec;126(6):563-70. PMID:16316975 doi:10.1085/jgp.200509417
- ↑ Dutzler R, Campbell EB, MacKinnon R. Gating the selectivity filter in ClC chloride channels. Science. 2003 Apr 4;300(5616):108-12. Epub 2003 Mar 20. PMID:12649487 doi:10.1126/science.1082708
- ↑ Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature. 2002 Jan 17;415(6869):287-94. PMID:11796999 doi:10.1038/415287a
- ↑ Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature. 2002 Jan 17;415(6869):287-94. PMID:11796999 doi:10.1038/415287a
- ↑ Jentsch TJ, Stein V, Weinreich F, Zdebik AA. Molecular structure and physiological function of chloride channels. Physiol Rev. 2002 Apr;82(2):503-68. PMID:11917096 doi:10.1152/physrev.00029.2001
