Difference between revisions of "Part:BBa K3396001"

 
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<partinfo>BBa_K3396001 short</partinfo>
 
<partinfo>BBa_K3396001 short</partinfo>
  
The Coch2 module binds DocS (BBa_K3396000) modules constitutively.  
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The Coh2 module binds DocS (BBa_K3396000) modules constitutively.  
  
 
===Usage and Biology===
 
===Usage and Biology===
  
The Coch2[1] module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary DocS modules harbored by each of the catalytic subunits. They can be used as a proof-of-concept tool to demonstrate whether a split-protein approach works. These pairs can also be replaced with other inducible protein dimerization pairs for signal-controlled purposes.
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The Coh2[1] module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary DocS modules harbored by each of the catalytic subunits. The Coh2–DocS pair represents the interaction between two complementary families of protein modules that exhibit divergent specificities and affinities, ranging from one of the highest known affinity constants between two proteins to relatively low-affinity interactions.
  
  

Latest revision as of 02:13, 28 October 2020


Coh2

The Coh2 module binds DocS (BBa_K3396000) modules constitutively.

Usage and Biology

The Coh2[1] module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary DocS modules harbored by each of the catalytic subunits. The Coh2–DocS pair represents the interaction between two complementary families of protein modules that exhibit divergent specificities and affinities, ranging from one of the highest known affinity constants between two proteins to relatively low-affinity interactions.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Reference

[1] BARAK Y, HANDELSMAN T, NAKAR D, et al. Matching fusion protein systems for affinity analysis of two interacting families of proteins: the cohesin-dockerin interaction [J]. J Mol Recognit, 2005, 18(6): 491-501.