The structural basis for membrane binding and pore formation by lymphocyte perforin

Ruby H. P. Law, Natalya Lukoyanova, Ilia Voskoboinik, Tom T. Caradoc-Davies, Katherine Baran, Michelle A. Dunstone, Michael E. D’Angelo, Elena V. Orlova, Fasséli Coulibaly, Sandra Verschoor, Kylie A. Browne, Annette Ciccone, Michael J. Kuiper, Phillip I. Bird, Joseph A. Trapani (), Helen R. Saibil () and James C. Whisstock ()
Additional contact information
Ruby H. P. Law: Monash University, Clayton, Melbourne, Victoria 3800, Australia
Natalya Lukoyanova: Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, UK
Ilia Voskoboinik: Cancer Immunology Program, Peter MacCallum Cancer Centre, St Andrew's Place, East Melbourne, Victoria 3002, Australia
Tom T. Caradoc-Davies: Australian Synchrotron, 800 Blackburn Road, Clayton, Melbourne, Victoria 3168, Australia
Katherine Baran: Cancer Immunology Program, Peter MacCallum Cancer Centre, St Andrew's Place, East Melbourne, Victoria 3002, Australia
Michelle A. Dunstone: Monash University, Clayton, Melbourne, Victoria 3800, Australia
Michael E. D’Angelo: Monash University, Clayton, Melbourne, Victoria 3800, Australia
Elena V. Orlova: Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, UK
Fasséli Coulibaly: Monash University, Clayton, Melbourne, Victoria 3800, Australia
Sandra Verschoor: Cancer Immunology Program, Peter MacCallum Cancer Centre, St Andrew's Place, East Melbourne, Victoria 3002, Australia
Kylie A. Browne: Cancer Immunology Program, Peter MacCallum Cancer Centre, St Andrew's Place, East Melbourne, Victoria 3002, Australia
Annette Ciccone: Cancer Immunology Program, Peter MacCallum Cancer Centre, St Andrew's Place, East Melbourne, Victoria 3002, Australia
Michael J. Kuiper: Victorian Partnership of Advanced Computing, Carlton South, Victoria 3053, Australia
Phillip I. Bird: Monash University, Clayton, Melbourne, Victoria 3800, Australia
Joseph A. Trapani: Cancer Immunology Program, Peter MacCallum Cancer Centre, St Andrew's Place, East Melbourne, Victoria 3002, Australia
Helen R. Saibil: Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, UK
James C. Whisstock: Monash University, Clayton, Melbourne, Victoria 3800, Australia

Nature, 2010, vol. 468, issue 7322, 447-451

Abstract: Perforin and pore formation The pore-forming immunity protein perforin, which is essential for the elimination of virally infected and cancerous cells, is released by natural killer and cytotoxic T cells. The structure of a perforin monomer — mouse perforin R213E — has now been determined. Analysis of the structure, together with a cryo-electron microscopy reconstruction of the oligomeric pore, suggests that perforin monomers within the pore adopt an 'inside-out' orientation compared with the structurally homologous monomers of cholesterol-dependent cytolysins. This novel adaptation may explain how perforin delivers pro-apoptotic proteases (granzymes) into target cells and how related complement immunity proteins assemble into pores.

Date: 2010
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DOI: 10.1038/nature09518

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