Overview
- Editors:
-
-
Gregor Anderluh
-
Department of Biology, University of Ljubljana, Ljubljana, Slovenia
-
Jeremy Lakey
-
Institute for Cell and Molecular Biosciences, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne, UK
- Novel structures and biophysical studies on proteins
- Includes a comparison of the properties of membrane channels formed by amyloid proteins and pore forming toxins
- Gives comprehensive overview of what we know about proteins and highlights their general structural properties
Access this book
Other ways to access
Table of contents (13 chapters)
-
-
- Susanne C. Feil, Galina Polekhina, Michael A. Gorman, Michael W. Parker
Pages 1-13
-
-
-
- Gustavo Fuertes, Diana Giménez, Santi Esteban-Martín, Ana J. García-Sáez, Orlando Sánchez, Jesús Salgado
Pages 31-55
-
-
- José Miguel Mancheño, Hiroaki Tateno, Daniel Sher, Irwin J. Goldstein
Pages 67-80
-
- Helen Ridleya, Christopher L. Johnson, Jeremy H. Lakey
Pages 81-90
-
- Ana J. García-Sáez, Gustavo Fuertes, Jacob Suckale, Jesús Salgado
Pages 91-105
-
- Biserka Bakrač, Gregor Anderluh
Pages 106-115
-
- Stuart Hunt, Jeffrey Green, Peter J. Artymiuk
Pages 116-126
-
- Mario Soberón, Liliana Pardo, Carlos Muñóz-Garay, Jorge Sánchez, Isabel Gómez, Helena Porta et al.
Pages 127-142
-
- Wen-guey Wu, Siu-Cin Tjong, Po-long Wu, Je-hung Kuo, Karen Wu
Pages 143-149
-
- Bruce L. Kagan, Jyothi Thundimadathil
Pages 150-167
-
Back Matter
Pages 169-172
About this book
Formation of transmembrane pores is a very effective way of killing cells. It is thus not surprising that many bacterial and eukaryotic toxic agents are pore-forming proteins. Pore formation in a target membrane is a complex process composed of several steps; proteins need to attach to the lipid membrane, possibly aggregate in the plane of the membrane and finally form a pore by inserting part of the polypeptide chain across the lipid bilayer. Structural information about toxins at each stage is indispensible for the biochemical and molecular biological studies that aim to - derstand how pores are formed at the molecular level. There are currently only two Staphylococcus aureus and hemolysin E from Escherichia coli. Therefore, 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 bi- ing 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.
Editors and Affiliations
-
Department of Biology, University of Ljubljana, Ljubljana, Slovenia
Gregor Anderluh
-
Institute for Cell and Molecular Biosciences, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne, UK
Jeremy Lakey
About the editors
Gregor Anderluh is Associate Professor of Biochemistry at the Department of Biology, Biotechnical Faculty, University of Ljubljana, Ljubljana,
Slovenia. He and his coworkers are studying protein-membrane interactions and how cellular membranes are damaged by proteins. He is a director of the Infrastuctural
Centre for Surface Plasmon Resonance at the University of Ljubljana, where they study molecular interactions and are developing novel approaches on how to study protein binding to membranes. He received his PhD in Biology from University of Ljubljana and did his Postdoctoral at University of Newcastle, United Kingdom.
Jeremy Lakey is Professor of Structural Biochemistry at the Institute for Cell and Molecular Biosciences, University of Newcastle, UK and runs an academic research group based loosely on the theme of protein biophysical chemistry with interests in protein toxins, membranes and bionanotechnology. Following a first degree in Zoology, Jeremy completed a PhD in Membrane Biophysics at the University of East Anglia UK, followed by periods at the Centre de Biophysique Moléculaire, Orléans, France; EMBL, Heidelberg, Germany and the EPFL , Lausanne Switzerland. He is currently an editor of the Biochemical Journal and member of the facility access panel for the ISIS pulsed neutron source, UK.
