Relevance of Lysine Snorkeling in the Outer Transmembrane Domain of Small Viral Potassium Ion Channels (Articolo in rivista)

Type
Label
  • Relevance of Lysine Snorkeling in the Outer Transmembrane Domain of Small Viral Potassium Ion Channels (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/bi3006016 (literal)
Alternative label
  • Gebhardt M; Henkes LM; Tayefeh S; Hertel B; Greiner T; Van Etten JL; Baumeister D; Cosentino C; Moroni A; Kast SM; Thiel G (2012)
    Relevance of Lysine Snorkeling in the Outer Transmembrane Domain of Small Viral Potassium Ion Channels
    in Biochemistry (Easton); American Chemical Society, Washington (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Gebhardt M; Henkes LM; Tayefeh S; Hertel B; Greiner T; Van Etten JL; Baumeister D; Cosentino C; Moroni A; Kast SM; Thiel G (literal)
Pagina inizio
  • 5571 (literal)
Pagina fine
  • 5579 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://pubs.acs.org/doi/abs/10.1021/bi3006016 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 51 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 28 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Tech Univ Darmstadt, Inst Bot, D-64287 Darmstadt, Germany; Univ Nebraska, Dept Plant Pathol, Lincoln, NE 68583 USA; Univ Nebraska, Nebraska Ctr Virol, Lincoln, NE 68583 USA; Tech Univ Dortmund, Dortmund, Germany; Univ Milan, CNR IBF Mi, Milan, Italy; Univ Milan, Dept Biol, Milan, Italy; Tech Univ Darmstadt, Darmstadt, Germany (literal)
Titolo
  • Relevance of Lysine Snorkeling in the Outer Transmembrane Domain of Small Viral Potassium Ion Channels (literal)
Abstract
  • Transmembrane domains (TMDs) are often flanked by Lys or Arg because they keep their aliphatic parts in the bilayer and their charged groups in the polar interface. Here we examine the relevance of this so-called \"snorkeling\" of a cationic amino acid, which is conserved in the outer TMD of small viral K+ channels. Experimentally, snorkeling activity is not mandatory for KcvPBCV-1 because K29 can be replaced by most of the natural amino acids without any corruption of function. Two similar channels, KcvATCV-1 and KcvMT325, lack a cytosolic N-terminus, and neutralization of their equivalent cationic amino acids inhibits their function. To understand the variable importance of the cationic amino acids, we reanalyzed molecular dynamics simulations of KcvPBCV-1 and N-terminally truncated mutants; the truncated mutants mimic KcvATCV-1 and KcvMT325. Structures were analyzed with respect to membrane positioning in relation to the orientation of K29. The results indicate that the architecture of the protein (including the selectivity filter) is only weakly dependent on TMD length and protonation of K29. The penetration depth of Lys in a given protonation state is independent of the TMD architecture, which leads to a distortion of shorter proteins. The data imply that snorkeling can be important for K+ channels; however, its significance depends on the architecture of the entire TMD. The observation that the most severe N-terminal truncation causes the outer TMD to move toward the cytosolic side suggests that snorkeling becomes more relevant if TMDs are not stabilized in the membrane by other domains. (literal)
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