Dataset

Defining the interaction of perforin with calcium and the phospholipid membrane

Monash University
Prof James Whisstock (Associated with)
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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=https://store.synchrotron.org.au/experiment/view/208/#metadata&rft.title=Defining the interaction of perforin with calcium and the phospholipid membrane&rft.identifier=https://store.synchrotron.org.au/experiment/view/208/#metadata&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. Beamline: MX2 EPN: 4297 PDB: 3W56 Organisim: Scophthalmus maximus   Expression System: Escherichia coli   Sequence: >3W56:A|PDBID|CHAIN|SEQUENCE MRGSHHHHHHENLYFQGQNSHMQLRLYNLRVRGLPSDLMGITDGYVKVFCGSANLGETSVNHNNANPWWTEEFSHFKAQE NDILRLEVHDEDTFFDDLLGVCQRQIKVGTHEHDCYLKEGGTLHYMYTLSV   &rft.creator=Anonymous&rft.date=2014&rft.relation=10.1042/BJ20130999&rft_rights=This experiment data is licensed under Creative Commons Attribution 3.0 Australia (CC BY 3.0). http://creativecommons.org/licenses/by/3.0/au/&rft_subject=OTHER PHYSICAL SCIENCES&rft_subject=PHYSICAL SCIENCES&rft_subject=Synchrotrons; Accelerators; Instruments and Techniques&rft_subject=Scophthalmus maximus &rft_subject=Escherichia coli &rft_subject=Macromolecular Crystallography&rft_subject=MX2&rft.type=dataset&rft.language=English Access the data

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This experiment data is licensed under Creative Commons Attribution 3.0 Australia (CC BY 3.0).
http://creativecommons.org/licenses/by/3.0/au/

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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.

  • Beamline: MX2
  • EPN: 4297
  • PDB: 3W56
  • Organisim: Scophthalmus maximus  
  • Expression System: Escherichia coli  
  • Sequence: >3W56:A|PDBID|CHAIN|SEQUENCE MRGSHHHHHHENLYFQGQNSHMQLRLYNLRVRGLPSDLMGITDGYVKVFCGSANLGETSVNHNNANPWWTEEFSHFKAQE NDILRLEVHDEDTFFDDLLGVCQRQIKVGTHEHDCYLKEGGTLHYMYTLSV  

Available: 25 03 2014

Data time period: 25 03 2014

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