期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 102, 期 40, 页码 14278-14283出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0501234102
关键词
amyloid-beta; membrane channel; membrane protein structure; prion; transmembrane helix
资金
- NIGMS NIH HHS [R01 GM063919-05, R01 GM063919, R01 GM063919-07, R01 GM063919-06, GM3919, R01 GM063919-08] Funding Source: Medline
We have observed a common sequence motif in membrane proteins, which we call a glycine zipper. Glycine zipper motifs are strongly overrepresented and conserved in membrane protein sequences, and mutations in glycine zipper motifs are deleterious to function in many cases. The glycine zipper has a significant structural impact, engendering a strong driving force for right-handed packing against a neighboring helix. Thus, the presence of a glycine zipper motif leads directly to testable structural hypotheses, particularly for a subclass of glycine zipper proteins that form channels. For example, we suggest that the membrane pores formed by the amyloid-beta peptide in vitro are constructed by glycine zipper packing and find that mutations in the glycine zipper motif block channel formation. Our findings highlight an important structural motif in a wide variety of normal and pathological processes.
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