Domain Organization of Long Signal Peptides of Single-Pass Integral Membrane Proteins Reveals Multiple Functional Capacity

@article{Hiss2008DomainOO,
  title={Domain Organization of Long Signal Peptides of Single-Pass Integral Membrane Proteins Reveals Multiple Functional Capacity},
  author={Jan A. Hiss and Eduard Resch and Alexander Schreiner and Michael Meissner and Anna Starzinski-Powitz and Gisbert Schneider},
  journal={PLoS ONE},
  year={2008},
  volume={3},
  pages={303 - 344}
}
Targeting signals direct proteins to their extra- or intracellular destination such as the plasma membrane or cellular organelles. Here we investigated the structure and function of exceptionally long signal peptides encompassing at least 40 amino acid residues. We discovered a two-domain organization ("NtraC model") in many long signals from vertebrate precursor proteins. Accordingly, long signal peptides may contain an N-terminal domain (N-domain) and a C-terminal domain (C-domain) with… CONTINUE READING

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Signal-3L: A 3-layer approach for predicting signal peptides.

Biochemical and biophysical research communications • 2007

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