Or use your Academic/Social account:
Congratulations!
You have just completed your registration at OpenAire.
Before you can login to the site, you will need to activate your account. An e-mail will be sent to you with the proper instructions.
Important!
Close This Message
Please note that this site is currently undergoing Beta testing.
Any new content you create is not guaranteed to be present to the final version
of the site upon release.
Thank you for your patience,
OpenAire Dev Team.
Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins
- Title
- Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins
- Funding
- ARC | Discovery Projects
- Contract (GA) number
- DP0986811
- Start Date
- 2009/01/01
- End Date
- 2011/12/31
- Open Access mandate
- no
- Organizations
- -
- More information
- http://purl.org/au-research/grants/arc/DP0986811
-
A New Model for Pore Formation by Cholesterol-Dependent Cytolysins
Reboul, Cyril F.; Whisstock, James C.; Dunstone, Michelle A. (2014)
Projects: ARC | ARC Centres of Excellences - Grant ID: CE140100011 (CE140100011), ARC | Membrane Attack Complex / Perforin like proteins in Defence, Attack and Developmental Biology (FF0883418), ARC | Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins (DP0986811), ARC | The mechanism of pore formation by Membrane Attack Complex/Perforin-like proteins (DP120104058), NHMRC | The role of membrane attack complex - perforin like pore foaming proteins in disease and immunity (606471)Cholesterol Dependent Cytolysins (CDCs) are important bacterial virulence factors that form large (200-300 Å) membrane embedded pores in target cells. Currently, insights from X-ray crystallography, biophysical and single particle cryo-Electron Microscopy (cryo-EM) experiments suggest that soluble monomers first interact with the membrane surface via a C-terminal Immunoglobulin-like domain (Ig; Domain 4). Membrane bound oligomers then assemble into a prepore oligomeric form, following which t...Conformational Changes during Pore Formation by the Perforin-Related Protein Pleurotolysin
Lukoyanova, Natalya; Kondos, Stephanie C.; Farabella, Irene; Law, Ruby H. P.; Reboul, Cyril F.; Caradoc-Davies, Tom T.; Spicer, Bradley A.; Kleifeld, Oded; Traore, Daouda A. K.; Ekkel, Susan M.; Voskoboinik, Ilia; Trapani, Joseph A.; Hatfaludi, Tamas; Oliver, Katherine; Hotze, Eileen M.;... (2015)
Projects: EC | MEMBRANEATTACK (294408), NIH | Pore Formation by Cholesterol Dependent Cytolysins (2R01AI037657-05), NHMRC | The role of membrane attack complex - perforin like pore foaming proteins in disease and immunity (606471), ARC | ARC Centres of Excellences - Grant ID: CE140100011 (CE140100011), ARC | The mechanism of pore formation by Membrane Attack Complex/Perforin-like proteins (DP120104058), ARC | Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins (DP0986811), WT | Cryo-electron microscopy equipment for structure determination of macromolecular and cellular assemblies. (079605), RCUK | Tools for Generating and Assessing Pseudo-atomic Models from 3D Electron Microscopy Maps of Macromolecular Assemblies. (BB/K01692X/1)Membrane attack complex/perforin-like (MACPF) proteins comprise the largest superfamily of pore-forming proteins, playing crucial roles in immunity and pathogenesis. Soluble monomers assemble into large transmembrane pores via conformational transitions that remain to be structurally and mechanistically characterised. Here we present an 11 Å resolution cryo-electron microscopy (cryo-EM) structure of the two-part, fungal toxin Pleurotolysin (Ply), together with crystal structures of both compo... -
No project research data found
-
Scientific Results
Chart is loading... It may take a bit of time. Please be patient and don't reload the page.
PUBLICATIONS BY ACCESS MODE
Chart is loading... It may take a bit of time. Please be patient and don't reload the page.
Publications in Repositories
Chart is loading... It may take a bit of time. Please be patient and don't reload the page.
