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Titolo:
Structure of the transmembrane region of the M2 protein H+ channel
Autore:
Wang, JF; Kim, S; Kovacs, F; Cross, TA;
Indirizzi:
Florida State Univ, Nath High Magnet Field Lab, Tallahassee, FL 32310 USA Florida State Univ Tallahassee FL USA 32310 ab, Tallahassee, FL 32310 USA Florida State Univ, Dept Chem, Tallahassee, FL 32310 USA Florida State Univ Tallahassee FL USA 32310 em, Tallahassee, FL 32310 USA Florida State Univ, Inst Mol Biophys, Tallahassee, FL 32310 USA Florida State Univ Tallahassee FL USA 32310 ys, Tallahassee, FL 32310 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 11, volume: 10, anno: 2001,
pagine: 2241 - 2250
SICI:
0961-8368(200111)10:11<2241:SOTTRO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
INFLUENZA-A VIRUS; SOLID-STATE NMR; INTEGRAL MEMBRANE-PROTEIN; PHASE PEPTIDE-SYNTHESIS; M-2 ION-CHANNEL; ORIENTATIONAL CONSTRAINTS; LIPID BILAYER; GRAMICIDIN-A; POLYPEPTIDE; DOMAIN;
Keywords:
influenza A; membrane protein structure; M2 proton channel; solid-state NMR; PISEMA; PISA wheel; orientational restraints;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Cross, TA Florida State Univ, Nath High Magnet Field Lab, 1800 E Paul Dirac Dr, Tallahassee, FL 32310 USA Florida State Univ 1800 E Paul Dirac Dr Tallahassee FL USA 32310
Citazione:
J.F. Wang et al., "Structure of the transmembrane region of the M2 protein H+ channel", PROTEIN SCI, 10(11), 2001, pp. 2241-2250

Abstract

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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Documento generato il 30/05/20 alle ore 15:16:14