User:Amy Kerzmann/Sandbox 4

From Proteopedia

< User:Amy Kerzmann(Difference between revisions)
Jump to: navigation, search
Current revision (01:07, 6 October 2009) (edit) (undo)
 
Line 1: Line 1:
-
== Voltage-Gated Calcium Channels ==
+
== Chloride Ion Channel ==
-
<applet load='1t0j' size='300' frame='true' align='left'
+
-
caption='VOLTAGE-GATED CALCIUM CHANNNEL' />
+
Crystal structure of a soluble form of CLIC1. An intracellular chloride ion channel
-
 
+
-
Voltage-gated calcium channels play crucial roles in many bodily functions
+
<applet load='1k0o' size='300' frame='true' align='right' caption='Insert caption here' />
-
including: cardiac action potentials, neurotransmitter release, muscle
+
-
contraction. During neurological functions, these calcium channels create
+
CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4-A resolution. The protein is monomeric and structurally homologous to the glutathione S-transferase superfamily, and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain (residues 1-90), with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes.
-
action potentials. At resting state,voltage-gated calcium channels are in a
+
Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution.
-
closed conformation. When the membrane is depolarized, they are open. The
+
-
pore-forming α1-subunit of voltage-gated Ca2+ channels (Cav)2 is composed of
+
-
four homologous domains (I-IV), each of which has six transmembrane segments
+
== About this Structure ==
-
(S1–S6). These channels initiate the release of neurotransmitters at
+
-
synapses, and have a powerful influence on synaptic strength. The nervous
+
-
system requires different levels of calcium concentration, so when
+
-
transmitter release occurs, high levels of calcium are needed. During
+
1K0O is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
-
short-term facilitation, slow steady streams of calcium build up. Failure
+
[edit]
-
of these calcium channels can result in migranes, ataxia, and also other
+
-
neurological diseases. Calmodulin is a specific calcium channel sensor, and
+
-
regulates the functions of the channel. Calcium binding to calmodulin
+
== References ==
-
regulates the facilitation of Ca2+ through the coltage-gated channels.
+
-
 
+
<references/>
-
----
+
-
 
+
<ref>PMID:#11551966</ref>
-
== Structure ==
+
-
This specific protein is a two chain structure and was first found in Rattus
+
Harrop SJ, DeMaere MZ, Fairlie WD, Reztsova T, Valenzuela SM, Mazzanti M, Tonini R, Qiu MR, Jankova L, Warton K, Bauskin AR, Wu WM, Pankhurst S, Campbell TJ, Breit SN, Curmi PM. Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution. J Biol Chem. 2001 Nov 30;276(48):44993-5000. Epub 2001 Sep 10. PMID:11551966
-
norvegicus.
+
-
 
+
-
The beta-interaction domain (BID), formed the AID-binding site; however,
+
-
this region is buried in the Ca(V)beta core and is unavailable for
+
-
protein-protein interactions.
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
----
+
-
[http://www.ncbi.nlm.nih.gov/pubmed/17052221]
+
-
[[http://www.ncbi.nlm.nih.gov/pubmed/18817729?ordinalpos=1=EntrezSyste <http://www.ncbi.nlm.nih.gov/pubmed/18817729?ordinalpos=1&itool=EntrezSyste>
+
-
m2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_Title
+
-
Search&linkpos=1&log$=pmtitlesearch4]]
+
-
[[http://www.ncbi.nlm.nih.gov/pubmed/18817727?ordinalpos=1=EntrezSyste <http://www.ncbi.nlm.nih.gov/pubmed/18817727?ordinalpos=1&itool=EntrezSyste>
+
-
m2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery
+
-
_RA&linkpos=1&log$=relatedreviews&logdbfrom=pubmed]]
+
-
[[http://www.jbc.org/content/282/6/3864.full]]
+
-
[[Catterall, W. A., Perez-Reyes, E., Snutch, T. P., and Striessnig, J.
+
-
(2005) Pharmacol. Rev. 57, 411-425Abstract/FREE Full Text]]
+
-
[http://www.ncbi.nlm.nih.gov/pubmed/16369047?ordinalpos=1=EntrezSystem <http://www.ncbi.nlm.nih.gov/pubmed/16369047?ordinalpos=1&itool=EntrezSystem>
+
-
2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_
+
-
RA&linkpos=1&log$=relatedreviews&logdbfrom=pubmed]
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
 
+
-
<scene name='User:Kyle_Barrett/Voltage-gated_calcium_channel/1'>Polarity
+
-
model of voltage-gated calcium channel</scene>
+

Current revision

Chloride Ion Channel

Crystal structure of a soluble form of CLIC1. An intracellular chloride ion channel

Insert caption here

Drag the structure with the mouse to rotate

CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4-A resolution. The protein is monomeric and structurally homologous to the glutathione S-transferase superfamily, and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain (residues 1-90), with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes. Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution.


About this Structure

1K0O is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA. [edit]


References


[1]

Harrop SJ, DeMaere MZ, Fairlie WD, Reztsova T, Valenzuela SM, Mazzanti M, Tonini R, Qiu MR, Jankova L, Warton K, Bauskin AR, Wu WM, Pankhurst S, Campbell TJ, Breit SN, Curmi PM. Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution. J Biol Chem. 2001 Nov 30;276(48):44993-5000. Epub 2001 Sep 10. PMID:11551966

Proteopedia Page Contributors and Editors (what is this?)

Amy Kerzmann

Retrieved from "http://52.214.119.220/wiki/index.php/User:Amy_Kerzmann/Sandbox_4"
Personal tools