Publisher description for Proteins : membrane binding and pore formation / edited by Gregor Anderluh, Jeremy Lakey.

Bibliographic record and links to related information available from the Library of Congress catalog

Information from electronic data provided by the publisher. May be incomplete or contain other coding.

There are currently only two structures of pores available, of α-toxin from Staphylococcus aureus and hemolysin E from Escherichia coli. So what we know about these proteins was obtained over many years of intense experimentation. We have nevertheless, in the last couple of years, witnessed a significant rise in structural information on the soluble forms of pore-forming proteins. Surprisingly, many unexpected similarities with other proteins were noted, despite extremely low or insignificant sequence similarity. It appears that lipid membrane binding and formation of transmembrane channels is achieved in many cases by a limited repertoire of structures. This book describes how several of the important pore forming toxin families achieve membrane binding and which structural elements are used for formation of transmembrane pores. Our contributors have thus provided the means for a comparative analysis of several unrelated families.

Library of Congress subject headings for this publication:
Membrane proteins.
Membrane lipids.
Membrane Proteins -- physiology.
Cell Membrane Permeability.
Membrane Lipids -- physiology.
Peptides -- physiology.
Pore Forming Cytotoxic Proteins -- physiology.
Protein Binding.