000 03236nam a22004455i 4500
001 978-1-4419-6327-7
003 DE-He213
005 20140220084509.0
007 cr nn 008mamaa
008 110110s2010 xxu| s |||| 0|eng d
020 _a9781441963277
_9978-1-4419-6327-7
024 7 _a10.1007/978-1-4419-6327-7
_2doi
050 4 _aR-RZ
072 7 _aMBGR
_2bicssc
072 7 _aMED000000
_2bisacsh
082 0 4 _a610
_223
100 1 _aAnderluh, Gregor.
_eeditor.
245 1 0 _aProteins Membrane Binding and Pore Formation
_h[electronic resource] /
_cedited by Gregor Anderluh, Jeremy Lakey.
264 1 _aNew York, NY :
_bSpringer New York,
_c2010.
300 _aXIX, 172 p.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
490 1 _aAdvances in Experimental Medicine and Biology,
_x0065-2598 ;
_v677
505 0 _aEnergetics 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 -- Interfacial 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 Heparan Sulfates and Glycosphingolipids in the Pore Formation of Basic Polypeptides of Cobra Cardiotoxin -- Amyloid Peptide Pores and the Beta Sheet Conformation.
520 _aThere 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.
650 0 _aMedicine.
650 1 4 _aBiomedicine.
650 2 4 _aBiomedicine general.
650 2 4 _aMolecular Medicine.
700 1 _aLakey, Jeremy.
_eeditor.
710 2 _aSpringerLink (Online service)
773 0 _tSpringer eBooks
776 0 8 _iPrinted edition:
_z9781441963260
830 0 _aAdvances in Experimental Medicine and Biology,
_x0065-2598 ;
_v677
856 4 0 _uhttp://dx.doi.org/10.1007/978-1-4419-6327-7
912 _aZDB-2-SBL
999 _c110615
_d110615