Difference between revisions of "Part:BBa K2543006:Design"
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1. [https://www.uniprot.org/uniprot/P01730 UniProtKB - P01730 (CD4_HUMAN)] <br /> | 1. [https://www.uniprot.org/uniprot/P01730 UniProtKB - P01730 (CD4_HUMAN)] <br /> | ||
2. [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1524797/ Retrovirology. (2006) Association between disruption of CD4 receptor dimerization and increased human immunodeficiency virus type 1 entry] <br /> | 2. [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1524797/ Retrovirology. (2006) Association between disruption of CD4 receptor dimerization and increased human immunodeficiency virus type 1 entry] <br /> | ||
| − | 3. J Immunol. (2006) Evidence for a domain-swapped CD4 dimer as the coreceptor for binding to class II MHC. | + | 3. [https://www.ncbi.nlm.nih.gov/pubmed/16709847 J Immunol. (2006) Evidence for a domain-swapped CD4 dimer as the coreceptor for binding to class II MHC.] <br /> |
| − | 4. J Immunol. (2006) Triggering of T cell activation via CD4 dimers. | + | 4. [https://www.ncbi.nlm.nih.gov/pubmed/16622011 J Immunol. (2006) Triggering of T cell activation via CD4 dimers.] <br /> |
| − | 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. | + | 5. [https://www.ncbi.nlm.nih.gov/pubmed/24550395 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.] <br /> |
Latest revision as of 17:33, 8 October 2018
hCD4 extracellular domain / pSB1C3
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 1138
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 1189
- 1000INCOMPATIBLE 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.