"Cytolytic peptides and proteins: Is there a common structural motif?" by David M. Ojcius and John Ding-E. Young
 

Cytolytic peptides and proteins: Is there a common structural motif?

ORCiD

David M. Ojcius: 0000-0003-1461-4495

Department

Biomedical Sciences

Document Type

Article

Publication Title

Trends in Biochemical Sciences

ISSN

0968-0004

Volume

16

DOI

10.1016/0968-0004(91)90090-I

First Page

225

Last Page

229

Publication Date

1-1-1991

Abstract

Pore-forming proteins or peptides (PFP) have now been isolated from a wide array of species ranging from humans to bacteria. A great number of these toxins lyse cells through a ‘barrel-stave’ mechanism, in which monomers of the toxin bind to and insert into the target membrane and then aggregate like barrel staves surrounding a central, water-filled pore. An evaluation of the secondary structures suggests that common secondary structures may be employed by most of these toxic PFP.

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