1mp6

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(New page: 200px<br /><applet load="1mp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mp6" /> '''Structure of the transmembrane region of the...)
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[[Image:1mp6.jpg|left|200px]]<br /><applet load="1mp6" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Structure of the transmembrane region of the M2 protein H+ channel by solid state NMR spectroscopy'''<br />
'''Structure of the transmembrane region of the M2 protein H+ channel by solid state NMR spectroscopy'''<br />
==Overview==
==Overview==
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The transmembrane domain of the M2 protein from influenza A virus forms a, nearly uniform and ideal helix in a liquid crystalline bilayer, environment. The exposure of the hydrophilic backbone structure is, minimized through uniform hydrogen bond geometry imposed by the low, dielectric lipid environment. A high-resolution structure of the monomer, backbone and a detailed description of its orientation with respect to the, bilayer were achieved using orientational restraints from solid-state NMR., With this unique information, the tetrameric structure of this H(+), channel is constrained substantially. Features of numerous published, models are discussed in light of the experimental structure of the monomer, and derived features of the tetrameric bundle.
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The transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high-resolution structure of the monomer backbone and a detailed description of its orientation with respect to the bilayer were achieved using orientational restraints from solid-state NMR. With this unique information, the tetrameric structure of this H(+) channel is constrained substantially. Features of numerous published models are discussed in light of the experimental structure of the monomer and derived features of the tetrameric bundle.
==About this Structure==
==About this Structure==
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1MP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MP6 OCA].
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1MP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MP6 OCA].
==Reference==
==Reference==
Structure of the transmembrane region of the M2 protein H(+) channel., Wang J, Kim S, Kovacs F, Cross TA, Protein Sci. 2001 Nov;10(11):2241-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11604531 11604531]
Structure of the transmembrane region of the M2 protein H(+) channel., Wang J, Kim S, Kovacs F, Cross TA, Protein Sci. 2001 Nov;10(11):2241-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11604531 11604531]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cross, T.A.]]
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[[Category: Cross, T A.]]
[[Category: Kim, S.]]
[[Category: Kim, S.]]
[[Category: Kovacs, F.]]
[[Category: Kovacs, F.]]
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[[Category: solid state nmr]]
[[Category: solid state nmr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:36:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:33 2008''

Revision as of 11:57, 21 February 2008


1mp6

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Structure of the transmembrane region of the M2 protein H+ channel by solid state NMR spectroscopy

Overview

The transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high-resolution structure of the monomer backbone and a detailed description of its orientation with respect to the bilayer were achieved using orientational restraints from solid-state NMR. With this unique information, the tetrameric structure of this H(+) channel is constrained substantially. Features of numerous published models are discussed in light of the experimental structure of the monomer and derived features of the tetrameric bundle.

About this Structure

1MP6 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Structure of the transmembrane region of the M2 protein H(+) channel., Wang J, Kim S, Kovacs F, Cross TA, Protein Sci. 2001 Nov;10(11):2241-50. PMID:11604531

Page seeded by OCA on Thu Feb 21 13:57:33 2008

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