Prediction structure and protein homology studies give rise to two hypotheses for folding of the transmembrane domain of RG1, the regulatory subunit of the glycogen-associated protein phosphatase

Prediction structure and protein homology studies give rise to two hypotheses for folding of the transmembrane domain of RG1, the regulatory subunit of the glycogen-associated protein phosphatase. M. Souchet^a, I. Bertand^a, N. Jullian^b et A. Bril^a. ^aSmithkline Beecham Laboratoires Pharmaceutiques, Rennes
^bMolecular Simulations The serine/threonine protein phosphatase 1 is comprised of two subunits: a catalytic and a regulatory subunit. The C-ter stretch of the latter (RG1) shows a hydrophobic domain likely to be inserted into the lipid bilayer. To study the features of this domain of interest, we have used

Holley-Karplus structure prediction method associated with a prediction method of transmembrane domains
Protein homology study (3D alignment using InsightII)

The first method led to an alpha helix for this domain including a putative molecular recognition pattern whereas the second one gave rise to beta sheet-type folding..

These two results are consistent with transmembrane foldings reported in the literature and exemplified by GPCR and chloride channel ICln, respectively. Further experiments are necessary to specify the exact secondary structure of this C-ter stretch of the protein.

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