Membrane Protein Gymnastics

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Science  25 Jun 2010:
Vol. 328, Issue 5986, pp. 1644-1645
DOI: 10.1126/science.1193065

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The high-resolution crystal structures of many membrane proteins (1) have provided a detailed understanding of the fold they adopt within the membrane. However, how a nascent polypeptide chain inserts into the membrane and folds to attain its final structure and orientation (topology) are an enigma. On page 1698 of this issue, Seppälä et al. (2) describe how a protein with up to five transmembrane domains could flip in the membrane, thus allowing a misinserted protein to attain its correct orientation (see the figure).