Ion-channel-forming colicins

Current Opinion in Structural Biology

Volumn 8, Issue 4, 1998, Pages 525-533

  Stroud, Robert M ^a   Reiling, Kinkead ^a   Wiener, Michael ^b   Freymann, Douglas ^c  

^a U ^*  (United States)

^b NORTHWESTERN UNIVERSITY   (United States)

^c UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COLICIN; ION CHANNEL; OUTER MEMBRANE PROTEIN;

CRYSTAL STRUCTURE; ION TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; REVIEW;

EID: 0032143552     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80132-2     Document Type: Article

References (39)

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39. Sattler M, Liang H, Nettesheim D, Meadows RP, Harlan JE, Eberstadt M, Yoon HS, Shuker SB, Chang BS, Minn AJ, et al. Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. of outstanding interest Science. 275:1997;983-986 The molecular structure of a complex between the survival protein Bcl-xL and the death-promoting region of the Bcl-2-related protein Bak indicates that the Bak peptide adopts an amphipathic a helix that interacts with the channel-forming Bcl-xL through hydrophobic and electrostatic interactions. This shows the close similarity of the channel-forming colicins - colicin immunity protein system in bacteria, to the molecular system that regulates cell death in eukaryotes.