Difference between revisions of "Part:BBa K2632004"

Revision as of 00:28, 18 October 2018

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 pyroptosis. 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.

Reference

https://www.ncbi.nlm.nih.gov/nuccore/NC_016810

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

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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.
+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. 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.
 <h3>Reference</h3>