Data

Defining the interaction of perforin with calcium and the phospholipid membrane

Monash University
Daouda Traore (Aggregated by) James Whisstock (Aggregated by)
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=info:doi10.4225/03/57428b07d325e&rft.title=Defining the interaction of perforin with calcium and the phospholipid membrane&rft.identifier=https://doi.org/10.4225/03/57428b07d325e&rft.publisher=Monash University&rft.description=Following its secretion from cytotoxic lymphocytes into the immune synapse, perforin binds to target cell membranes through its Ca2 + -dependent C2 domain. Membrane-bound perforin then forms pores that allow passage of pro-apoptopic granzymes into the target cell. In the present study, structural and biochemical studiesrevealthatCa2+ bindingtriggersaconformationalchange in the C2 domain that permits four key hydrophobic residues to interact with the plasma membrane. However, in contrast with previous suggestions, these movements and membrane binding do not trigger irreversible conformational changes in the pore-forming MACPF (membrane attack complex/perforin- like) domain, indicating that subsequent monomer–monomer interactions at the membrane surface are required for perforin pore formation.&rft.creator=Daouda Traore&rft.creator=Daouda Traore&rft.creator=James Whisstock&rft.creator=James Whisstock&rft.date=2016&rft_rights=CC-BY-4.0&rft_subject=Granzymes&rft_subject=Perforin&rft_subject=ImagingLocus&rft_subject=Biochemistry&rft_subject=Molecular Biology&rft.type=dataset&rft.language=English Access the data
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Following its secretion from cytotoxic lymphocytes into the immune synapse, perforin binds to target cell membranes through its Ca2 + -dependent C2 domain. Membrane-bound perforin then forms pores that allow passage of pro-apoptopic granzymes into the target cell. In the present study, structural and biochemical studiesrevealthatCa2+ bindingtriggersaconformationalchange in the C2 domain that permits four key hydrophobic residues to interact with the plasma membrane. However, in contrast with previous suggestions, these movements and membrane binding do not trigger irreversible conformational changes in the pore-forming MACPF (membrane attack complex/perforin- like) domain, indicating that subsequent monomer–monomer interactions at the membrane surface are required for perforin pore formation.

Issued: 2016-05-23

Created: 2016-05-23

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Subjects
Biochemistry | Granzymes | ImagingLocus | Molecular Biology | Perforin |

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Identifiers
ACN 633 798 857