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

Author

Listed:
  • Ruby H. P. Law

    (Monash University, Clayton, Melbourne, Victoria 3800, Australia
    The ARC Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, 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
    The University of Melbourne, Parkville, Victoria 3010, 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
    Monash University, 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
    The University of Melbourne, Parkville, Victoria 3010, 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
    The ARC Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Melbourne, Victoria 3800, Australia)

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.

Suggested Citation

  • 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 &, 2010. "The structural basis for membrane binding and pore formation by lymphocyte perforin," Nature, Nature, vol. 468(7322), pages 447-451, November.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7322:d:10.1038_nature09518
    DOI: 10.1038/nature09518
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