1mp6
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp6 OCA], [http://www.ebi.ac.uk/pdbsum/1mp6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mp6 RCSB]</span> | ||
}} | }} | ||
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[[Category: solid state nmr]] | [[Category: solid state nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:09 2008'' |
Revision as of 19:19, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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