There are currently only two structures of pores available, of ?-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. Wehave 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 casesby a limited repertoire of structures. This book describes how several of theimportant 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 unrelatedfamilies. 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 INDICE: Introduction.- Energetics of Peptide and Protein Binding to Lipid Membranes.- Membrane Association and Pore Formation by Alpha?Helical Peptides.- Role of Membrane Lipids for the Activity of Pore Forming Peptides and Proteins.- Cholesterol?Dependent Cytolysins.- Laetiporus sulphureus Lectin and Aerolysin Protein Family.- Interfa cial Interactions of Pore-Forming Colicins.- Permeabilization of the Outer Mitochondrial Membrane by Bcl?2 Proteins.- Molecular Mechanism of Sphingomyelin?Specific Membrane Binding and Pore Formation by Actinoporins.- Hemolysin E (HlyE, ClyA, SheA) and Related Toxins.- Pore formation by Cry toxins.- Role of Hepa ran Sulfa tes and Glycosphingolipids in the Pore Formation of Basic Polypeptides of Cobra Cardiotoxin.- Amyloid Peptide Pores and The Beta Sheet Conformation
- ISBN: 978-1-4419-6326-0
- Editorial: Springer
- Encuadernacion: Cartoné
- Páginas: 150
- Fecha Publicación: 05/07/2010
- Nº Volúmenes: 1
- Idioma: Inglés