Difference between revisions of "Part:BBa K2543006:Design"
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===References===
 
===References===
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1. [https://www.uniprot.org/uniprot/P01730 UniProtKB - P01730 (CD4_HUMAN)]
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2. Retrovirology. (2006) Association between disruption of CD4 receptor dimerization and increased human immunodeficiency virus type 1 entry
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3. J Immunol. (2006) Evidence for a domain-swapped CD4 dimer as the coreceptor for binding to class II MHC.
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4. J Immunol. (2006) Triggering of T cell activation via CD4 dimers.
 +
5. J Biol Chem. (2014) Disulfide reduction in CD4 domain 1 or 2 is essential for interaction with HIV glycoprotein 120 (gp120), which impairs thioredoxin-driven CD4 dimerization.

Revision as of 17:30, 8 October 2018


hCD4 extracellular domain / pSB1C3


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 1138
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 1189
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 370


Design Notes

This part follows the RFC[25] assembly rule with an AgeI site in the 3' end.


Source

This part was synthesized by Integrated DNA Technologies, Inc. (IDT) and cloned onto pSB1C3.


References

1. UniProtKB - P01730 (CD4_HUMAN) 2. Retrovirology. (2006) Association between disruption of CD4 receptor dimerization and increased human immunodeficiency virus type 1 entry 3. J Immunol. (2006) Evidence for a domain-swapped CD4 dimer as the coreceptor for binding to class II MHC. 4. J Immunol. (2006) Triggering of T cell activation via CD4 dimers. 5. J Biol Chem. (2014) Disulfide reduction in CD4 domain 1 or 2 is essential for interaction with HIV glycoprotein 120 (gp120), which impairs thioredoxin-driven CD4 dimerization.