Difference between revisions of "Part:BBa K2632005"
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Pyroptosis is a form of lytic programmed cell death with inflammation. Recent studies reported that  N-terminal of Gasdermin D <a href="https://parts.igem.org/Part:BBa_K2632003">(BBa K2632003)</a> acts as a effector of pyroptosis. Full length Gasdermin D is cleaved by Caspase 1 then release the PFD (pore-forming domain) which can oligomerize on the cell membrane. Formation of pore causes cell swelling, rupture of the membrane and massive leakage of cytosolic contents. L290D mutation of full length Gasdermin D reduces the cell toxicity.
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Pyroptosis is a form of lytic programmed cell death with inflammation. Recent studies reported that  N-terminal of Gasdermin D <a href="https://parts.igem.org/Part:BBa_K2632003">(BBa K2632003)</a> acts as an effector of pyroptosis<up>1</up>. Full length Gasdermin D is cleaved by Caspase 1 and then release the PFD (pore-forming domain) which can oligomerize on the cell membrane. Formation of pores causes cell to swell, leading to rupture of the membrane and massive leakage of cytosolic contents. L290D mutation of full length Gasdermin D reduces the cell toxicity.
  
 
<h3>Reference</h3>
 
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Ding J, Wang K, Liu W, et al. Pore-forming activity and structural autoinhibition of the gasdermin family[J]. Nature, 2016, 535(7610):111.
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1. Ding J, Wang K, Liu W, et al. Pore-forming activity and structural autoinhibition of the gasdermin family[J]. Nature, 2016, 535(7610):111.
 
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Revision as of 00:37, 18 October 2018

L290D mutant of full length Gasdermin D

Pyroptosis is a form of lytic programmed cell death with inflammation. Recent studies reported that N-terminal of Gasdermin D (BBa K2632003) acts as an effector of pyroptosis1. Full length Gasdermin D is cleaved by Caspase 1 and then release the PFD (pore-forming domain) which can oligomerize on the cell membrane. Formation of pores causes cell to swell, leading to rupture of the membrane and massive leakage of cytosolic contents. L290D mutation of full length Gasdermin D reduces the cell toxicity.

Reference

1. Ding J, Wang K, Liu W, et al. Pore-forming activity and structural autoinhibition of the gasdermin family[J]. Nature, 2016, 535(7610):111.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 1204
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 883