Difference between revisions of "Part:BBa K5036033"
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+ | ==Software Characterization== | ||
+ | we had the chance to match the external domains with different internal domain components to select single suitable receptor chain. The whole chain affinity is affected by the internal domain, thus we had to try: | ||
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+ | VEGFR1Cdcas-VEGFA | ||
+ | <html><div align="center"style="border:solid #17252A; width:100%;float:center;"><img style=" max-width:850px; | ||
+ | width:75%; | ||
+ | height:auto; | ||
+ | position: relative; | ||
+ | top: 50%; | ||
+ | left: 35%; | ||
+ | transform: translate( -50%); | ||
+ | padding-bottom:25px; | ||
+ | padding-top:25px; | ||
+ | "src="https://static.igem.wiki/teams/5036/part-software/vegfr1cdcas9-vegfa.gif | ||
+ | "> | ||
+ | <p class=MsoNormal align=center style='text-align:left;border:none;width:98% ;justify-content:center;'><span | ||
+ | lang=EN style='padding-bottom:30px;font-size:11.0pt;line-height:115%'>The interaction between the chain composed of VEGFR1 as an external domain and Cdcas9 as an internal domain with VEGFA yields ΔG of -11.2 kcal mol-1 | ||
+ | . </span></p></div></html> | ||
<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here |
Revision as of 06:54, 25 September 2024
dCas9(C)_NLS-Syn-VEGFR-1 (VEGF-R1, N-TEV, NLS, TCS(Q,G),HA,dCas9(C),VP64,GFP)
Part Description
In our first receptor chain, we've engineered a system that responds to tissue injury. An external domain, VEGF-R1, is attached to an internal domain composed of N terminal domain of TEV protease, a nuclear localization signal (NLS), a TEV cleavage site(TCS(Q,G)), and dCas9(C) which is linked to transcription activator VP64
Usage
this is our receptor's first chain. our receptor is activated after binding of VEGF to the external domain which is designed to attach specifically to it. after activation the two domains of TEV dimerizes forming catalytically active TEV protease which will cleave the two chains at TCS. upon cleavage of the two chains the two domains of dCas9 dimerize and is released attached to transcription activator to be guided to its direction
This figure illustrates variant of our receptor's first chain where N-TEV is to it. . .
Software Characterization
we had the chance to match the external domains with different internal domain components to select single suitable receptor chain. The whole chain affinity is affected by the internal domain, thus we had to try:
VEGFR1Cdcas-VEGFA
The interaction between the chain composed of VEGFR1 as an external domain and Cdcas9 as an internal domain with VEGFA yields ΔG of -11.2 kcal mol-1 .
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 2173
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 3958
Illegal NgoMIV site found at 4031
Illegal NgoMIV site found at 4516
Illegal NgoMIV site found at 5425 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 6722
Illegal SapI.rc site found at 3274