The membrane topology of human transient receptor potential 3 as inferred from glycosylation-scanning mutagenesis and epitope immunocytochemistry.

@article{Vannier1998TheMT,
  title={The membrane topology of human transient receptor potential 3 as inferred from glycosylation-scanning mutagenesis and epitope immunocytochemistry.},
  author={B Vannier and Xinjun Cindy Zhu and Dennis L. Brown and Lutz Birnbaumer},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 15},
  pages={
          8675-9
        }
}
Transient receptor potential (Trp) proteins form ion channels implicated in the calcium entry observed after stimulation of the phospholipase C pathway. Kyte-Doolittle analysis of the amino acid sequence of Trp proteins identifies seven hydrophobic regions (H1-H7) with potential of forming transmembrane segments. A limited sequence similarity to voltage-gated calcium channel alpha1 subunits lead to the prediction of six transmembrane (TM) segments flanked by intracellular N and C termini and a… CONTINUE READING
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