User:Amy Kerzmann/Sandbox 4

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== M2 Proton Channel from ''Influenza'' A Virus ==
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== Chloride Ion Channel ==
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<applet load='1nyj' size='300' frame='true' align='right' caption='The closed state structure of M2 protein H+ channel by solid state NMR spectroscopy.'/>
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Crystal structure of a soluble form of CLIC1. An intracellular chloride ion channel
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== Background ==
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The M2 proton channel is a key protein that leads to viral infection [Takeuchi et al]. The M2 proton channel acidifies the viron which allows the viral matrix protein (M1) to disassociate from the ribonucleoprotein (RNP) [wu et al]. This allows the RNP to be transported to the nucleus of the cell [wu et al]. Several recent studies have looked at the effects of amantadine [Stouffer et al] and rimantadine [Schnell et al] on inhibiting the transfer of protons through the M2 channel [stouffer et al]. It has been found that M2 is resistant to these two drugs in 90% of humans, birds and pigs stouffer et al]. Understanding the structure and function of this proton channel is necessary in solving the resistance problem <ref>PMID:18235504</ref>.
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<applet load='1k0o' size='300' frame='true' align='right' caption='Insert caption here' />
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== Structure ==
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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.
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The M2 proton channel from influenza A is 97 amino acid residues and forms a 24-residue N-terminal extracellular domain, a 19-residue trans-membrane domain, and a 54-residue C-terminal cytoplasmic domain [wu et al]. The 19-residue TM domain forms the highly selective proton channel [Takashi et al]. Circular dichroism spectra has shown the TM domain to form one α-helix that spans the membrane [wu et al]. By analytical ultracentrifugation, the TM domain is found to form α-helical tetramers. This tetrameric bundle of the TM domain is found by NMR to be tilted by 25-38° from the channel axis [takeuchi et al]. The trameric helices form a left-handed bundle that resembles a truncated cone [Stouffer et al]. The TM helicies are arranged around the channel pore with an approximate fourfold rotational symmetry [takeuchi et al].
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Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution.
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== Central Cavity ==
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<applet load='3bkd' size='300' frame='true' align='right' caption='High resolution Crystal structure of Transmembrane domain of M2 protein [Stouffer et al]' />
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== About this Structure ==
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1K0O is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
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[edit]
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== pH Gating ==
 
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== References ==
== References ==
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<references />
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<references/>
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<ref>PMID:#11551966</ref>
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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

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

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