Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.

@article{Baker2007EnzymaticAO,
  title={Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.},
  author={Rosanna P. Baker and Keith E. Young and Liang Feng and Yigong Shi and Sini{\vs}a Urban},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 20},
  pages={
          8257-62
        }
}
Intramembrane proteolysis is a core regulatory mechanism of cells that raises a biochemical paradox of how hydrolysis of peptide bonds is accomplished within the normally hydrophobic environment of the membrane. Recent high-resolution crystal structures have revealed that rhomboid proteases contain a catalytic serine recessed into the plane of the membrane, within a hydrophilic cavity that opens to the extracellular face, but protected laterally from membrane lipids by a ring of transmembrane… CONTINUE READING
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Genome Biol 4:R19

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  • 2003
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