Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
Open Access
- 11 November 2008
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 105 (45), 17379-17383
- https://doi.org/10.1073/pnas.0807764105
Abstract
The structures of transmembrane pores formed by a large family of pore-forming proteins and peptides are unknown. These proteins, whose secondary structures are predominantly α-helical segments, and many peptides form pores in membranes without a crystallizable protein assembly, contrary to the family of β-pore-forming proteins, which form crystallizable β-barrel pores. Nevertheless, a protein-induced pore in membranes is commonly assumed to be a protein channel. Here, we show a type of peptide-induced pore that is not framed by a peptide structure. Peptide-induced pores in multiple bilayers were long-range correlated into a periodically ordered lattice and analyzed by X-ray diffraction. We found the pores induced by Bax-derived helical peptides were at least partially framed by a lipid monolayer. Evidence suggests that the formation of such lipidic pores is a major mechanism for α-pore-forming proteins, including apoptosis-regulator Bax.Keywords
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