This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1mp6
From Proteopedia
|
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 Tue Nov 20 21:36:01 2007
