Earlier this month, a study previously reported in our Conference News appeared in PNAS. Researchers led by structural biologist James Bowie at University of California, Los Angeles, report that a glycine zipper motif in membrane protein sequences creates a driving force for packing of those proteins against neighboring protein helices. Aβ channels or related structures might form in the process, Bowie suggests. Review the story from last year's NBA conference for a summary, context, and some commentary on the study, and write back with your comments.—Gabrielle Strobel.

Reference:
Kim S, Jeon TJ, Oberai A, Yang D, Schmidt JJ, Bowie JU. Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14278-83. Abstract

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References

News Citations

  1. Conformation Rules Part 2: News, Common Threads, Debate from San Diego Protein Misfolding Conference

Paper Citations

  1. . Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14278-83. PubMed.

Further Reading

Papers

  1. . Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14278-83. PubMed.

News

  1. Conformation Rules Part 2: News, Common Threads, Debate from San Diego Protein Misfolding Conference

Primary Papers

  1. . Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14278-83. PubMed.